6JVU

Crystal structure of Klebsiella pneumoniae CysE in complex with L-cysteine

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6jvua_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Serine acetyltransferase	automated matches	(Klebsiella pneumoniae MGH 78578 ) [TaxId: 1328388 ],	SCOPe (2.08)
B	d6jvub_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Serine acetyltransferase	automated matches	(Klebsiella pneumoniae MGH 78578 ) [TaxId: 1328388 ],	SCOPe (2.08)
C	d6jvuc_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Serine acetyltransferase	automated matches	(Klebsiella pneumoniae MGH 78578 ) [TaxId: 1328388 ],	SCOPe (2.08)
D	d6jvud_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Serine acetyltransferase	automated matches	(Klebsiella pneumoniae MGH 78578 ) [TaxId: 1328388 ],	SCOPe (2.08)
E	d6jvue_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Serine acetyltransferase	automated matches	(Klebsiella pneumoniae MGH 78578 ) [TaxId: 1328388 ],	SCOPe (2.08)
F	d6jvuf_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Serine acetyltransferase	automated matches	(Klebsiella pneumoniae MGH 78578 ) [TaxId: 1328388 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Serine acetyltransferase	8093777	4001889	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Trimeric LpxA-like enzymes	8093778	3001804	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8093778	3001804	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8093778	3001804	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8093778	3001804	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8093778	3001804	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8093778	3001804	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Hexapep_2_1	e6jvuA2	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: Hexapep_2_1	ECOD (1.6)
A	SATase_N	e6jvuA1	A: alpha arrays	X: Serine acetyltransferase N-terminal domain (From Topology)	H: Serine acetyltransferase N-terminal domain (From Topology)	T: Serine acetyltransferase N-terminal domain	F: SATase_N	ECOD (1.6)
B	Hexapep_2_1	e6jvuB2	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: Hexapep_2_1	ECOD (1.6)
B	SATase_N	e6jvuB1	A: alpha arrays	X: Serine acetyltransferase N-terminal domain (From Topology)	H: Serine acetyltransferase N-terminal domain (From Topology)	T: Serine acetyltransferase N-terminal domain	F: SATase_N	ECOD (1.6)
C	Hexapep_2_1	e6jvuC2	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: Hexapep_2_1	ECOD (1.6)
C	SATase_N	e6jvuC1	A: alpha arrays	X: Serine acetyltransferase N-terminal domain (From Topology)	H: Serine acetyltransferase N-terminal domain (From Topology)	T: Serine acetyltransferase N-terminal domain	F: SATase_N	ECOD (1.6)
D	Hexapep_2_1	e6jvuD1	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: Hexapep_2_1	ECOD (1.6)
D	SATase_N	e6jvuD2	A: alpha arrays	X: Serine acetyltransferase N-terminal domain (From Topology)	H: Serine acetyltransferase N-terminal domain (From Topology)	T: Serine acetyltransferase N-terminal domain	F: SATase_N	ECOD (1.6)
E	Hexapep_2_1	e6jvuE1	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: Hexapep_2_1	ECOD (1.6)
E	SATase_N	e6jvuE2	A: alpha arrays	X: Serine acetyltransferase N-terminal domain (From Topology)	H: Serine acetyltransferase N-terminal domain (From Topology)	T: Serine acetyltransferase N-terminal domain	F: SATase_N	ECOD (1.6)
F	Hexapep_2_1	e6jvuF1	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: Hexapep_2_1	ECOD (1.6)
F	SATase_N	e6jvuF2	A: alpha arrays	X: Serine acetyltransferase N-terminal domain (From Topology)	H: Serine acetyltransferase N-terminal domain (From Topology)	T: Serine acetyltransferase N-terminal domain	F: SATase_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.3130.10	Mainly Alpha	Orthogonal Bundle	serine acetyltransferase, domain 1	serine acetyltransferase, domain 1	CATH (utative)
A	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (utative)
B	1.10.3130.10	Mainly Alpha	Orthogonal Bundle	serine acetyltransferase, domain 1	serine acetyltransferase, domain 1	CATH (utative)
B	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (utative)
C	1.10.3130.10	Mainly Alpha	Orthogonal Bundle	serine acetyltransferase, domain 1	serine acetyltransferase, domain 1	CATH (utative)
C	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (utative)
D	1.10.3130.10	Mainly Alpha	Orthogonal Bundle	serine acetyltransferase, domain 1	serine acetyltransferase, domain 1	CATH (utative)
D	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (utative)
E	1.10.3130.10	Mainly Alpha	Orthogonal Bundle	serine acetyltransferase, domain 1	serine acetyltransferase, domain 1	CATH (utative)
E	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (utative)
F	1.10.3130.10	Mainly Alpha	Orthogonal Bundle	serine acetyltransferase, domain 1	serine acetyltransferase, domain 1	CATH (utative)
F	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00132	Bacterial transferase hexapeptide (six repeats) (Hexapep)	Bacterial transferase hexapeptide (six repeats)	-	Repeat
A, B, C, D, E A, B, C, D, E, F	PF06426	Serine acetyltransferase, N-terminal (SATase_N)	Serine acetyltransferase, N-terminal	The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants [2] and bacteria [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Serine acetyltransferase	acetyltransferase activity serine O-acyltransferase activity O-acyltransferase activity serine O-acetyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity O-acetyltransferase activity catalytic activity	serine family amino acid metabolic process oxoacid metabolic process sulfur amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process cysteine biosynthetic process small molecule metabolic process sulfur compound metabolic process cysteine biosynthetic process from serine small molecule biosynthetic process carboxylic acid metabolic process serine family amino acid metabolic process oxoacid metabolic process sulfur amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process cysteine biosynthetic process small molecule metabolic process sulfur compound metabolic process cysteine biosynthetic process from serine small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-serine metabolic process L-amino acid metabolic process cysteine metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process sulfur compound biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process serine family amino acid biosynthetic process sulfur amino acid biosynthetic process alpha-amino acid biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR045304	Serine acetyltransferase, LbH domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR042122	Serine acetyltransferase, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR010493	Serine acetyltransferase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR005881	Serine O-acetyltransferase	Family
A, B, C, D, E A, B, C, D, E, F	IPR053376	Serine acetyltransferase	Family
A, B, C, D, E A, B, C, D, E, F	IPR018357	Hexapeptide transferase, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR001451	Hexapeptide repeat	Repeat

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.