4JUT

Crystal structure of a mutant fragment of Human HSPB6

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Hsp20 chaperone-like	8089934	3001242	SCOP2B (2022-06-29)
C	SCOP2 Family	Alpha crystallin-like	8047852	4005849	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Hsp20 chaperone-like	8089934	3001242	SCOP2 (2022-06-29)
D	SCOP2B Superfamily	Hsp20 chaperone-like	8089934	3001242	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Hsp20 chaperone-like	8089934	3001242	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Hsp20 chaperone-like	8089934	3001242	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Hsp20 chaperone-like	8089934	3001242	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Hsp20 chaperone-like	8089934	3001242	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Hsp20 chaperone-like	8089934	3001242	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)
B	HSP20	e4jutB1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: HSP20	ECOD (1.6)
C	HSP20	e4jutC1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: HSP20	ECOD (1.6)
D	HSP20	e4jutD1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: HSP20	ECOD (1.6)
F	HSP20	e4jutF1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: HSP20	ECOD (1.6)
G	HSP20	e4jutG1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: HSP20	ECOD (1.6)
H	HSP20	e4jutH1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: HSP20	ECOD (1.6)
A	HSP20	e4jutA1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: HSP20	ECOD (1.6)
E	HSP20	e4jutE1	A: beta sandwiches	X: HSP20-like	H: HSP20-like chaperones (From Topology)	T: HSP20-like chaperones	F: HSP20	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
C	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
D	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
F	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
G	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
H	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
A	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
E	2.60.40.790	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF00011	Hsp20/alpha crystallin family (HSP20)	Hsp20/alpha crystallin family	Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts [2].	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, G, H	Heat shock protein beta-6	unfolded protein binding protein binding binding identical protein binding protein homodimerization activity protein dimerization activity structural molecule activity structural constituent of eye lens protein folding chaperone protein-folding chaperone binding	protein refolding primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process multicellular organismal process regulation of developmental process positive regulation of biological process protein refolding primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process multicellular organismal process regulation of developmental process positive regulation of biological process angiogenesis regulation of vasculature development positive regulation of developmental process multicellular organism development tube morphogenesis anatomical structure development regulation of multicellular organismal process regulation of anatomical structure morphogenesis blood vessel development system development developmental process regulation of multicellular organismal development regulation of biological process blood vessel morphogenesis tube development biological regulation positive regulation of angiogenesis vasculature development circulatory system development anatomical structure morphogenesis positive regulation of vasculature development regulation of angiogenesis anatomical structure formation involved in morphogenesis positive regulation of multicellular organismal process regulation of cellular process negative regulation of programmed cell death regulation of apoptotic process negative regulation of biological process regulation of programmed cell death cell death negative regulation of apoptotic process negative regulation of cellular process apoptotic process programmed cell death chaperone-mediated protein folding response to stimulus response to stress response to heat response to abiotic stimulus response to temperature stimulus	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle lumen nuclear speck nuclear body nucleoplasm membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle lumen nuclear speck nuclear body nucleoplasm organelle lumen nuclear lumen extracellular region cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002068	Alpha crystallin/Hsp20 domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR001436	Alpha crystallin/Small heat shock protein, animal type	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR003090	Alpha-crystallin, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR008978	HSP20-like chaperone	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H	Pharos: O14558	heart disease non-small cell lung carcinoma polycystic ovary syndrome Adverse reaction to drug dermatomyositis ductal breast carcinoma in situ lung cancer malignant mesothelioma myopathy ovarian cancer psoriasis atypical teratoid rhabdoid tumor Gaucher disease invasive ductal breast carcinoma malignant colon neoplasm heart disease non-small cell lung carcinoma polycystic ovary syndrome Adverse reaction to drug dermatomyositis ductal breast carcinoma in situ lung cancer malignant mesothelioma myopathy ovarian cancer psoriasis atypical teratoid rhabdoid tumor Gaucher disease invasive ductal breast carcinoma malignant colon neoplasm malignant pancreatic neoplasm nephrotic syndrome pancreatic ductal adenocarcinoma breast carcinoma glioblastoma large cell medulloblastoma malignant glioma medulloblastoma

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.