5AZU

CRYSTAL STRUCTURE ANALYSIS OF OXIDIZED PSEUDOMONAS AERUGINOSA AZURIN AT PH 5.5 AND PH 9.0. A PH-INDUCED CONFORMATIONAL TRANSITION INVOLVES A PEPTIDE BOND FLIP

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	d5azua_	All beta proteins	Cupredoxin-like	Cupredoxins	Plastocyanin/azurin-like	Azurin	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
C	d5azuc_	All beta proteins	Cupredoxin-like	Cupredoxins	Plastocyanin/azurin-like	Azurin	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
D	d5azud_	All beta proteins	Cupredoxin-like	Cupredoxins	Plastocyanin/azurin-like	Azurin	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
B	d5azub_	All beta proteins	Cupredoxin-like	Cupredoxins	Plastocyanin/azurin-like	Azurin	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cupredoxins	8037683	3000886	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Cupredoxins	8037683	3000886	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Cupredoxins	8037683	3000886	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cupredoxins	8037683	3000886	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	Copper-bind	e5azuA1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Copper-bind	ECOD (1.6)
C	Copper-bind	e5azuC1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Copper-bind	ECOD (1.6)
D	Copper-bind	e5azuD1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Copper-bind	ECOD (1.6)
B	Copper-bind	e5azuB1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Copper-bind	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
C	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
D	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
B	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00127	Copper binding proteins, plastocyanin/azurin family (Copper-bind)	Copper binding proteins, plastocyanin/azurin family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	AZURIN	cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding zinc ion binding electron transfer activity identical protein binding protein binding	-	cellular anatomical structure periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR050845	Copper-binding electron transfer protein	Family
A, B, C, D	IPR000923	Blue (type 1) copper domain	Domain
A, B, C, D	IPR028871	Blue (type 1) copper protein, binding site	Binding Site
A, B, C, D	IPR008972	Cupredoxin	Homologous Superfamily
A, B, C, D	IPR014068	Azurin	Family

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.