3Q9E
Crystal structure of H159A APAH complexed with acetylspermine
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
B | SCOP2 Family | HDAC-like | 8099453 | 4000427 | SCOP2 (2022-06-29) |
B | SCOP2 Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2 (2022-06-29) |
C | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
J | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
K | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
E | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
F | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
G | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
H | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
I | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | SCOP2B (2022-06-29) |
L | SCOP2B Superfamily | Arginase/deacetylase-like | 8099454 | 3000260 | 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 | Hist_deacetyl | e3q9eB1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
C | Hist_deacetyl | e3q9eC1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
D | Hist_deacetyl | e3q9eD1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
J | Hist_deacetyl | e3q9eJ1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
K | Hist_deacetyl | e3q9eK1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
A | Hist_deacetyl | e3q9eA1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
E | Hist_deacetyl | e3q9eE1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
F | Hist_deacetyl | e3q9eF1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
G | Hist_deacetyl | e3q9eG1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
H | Hist_deacetyl | e3q9eH1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
I | Hist_deacetyl | e3q9eI1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
L | Hist_deacetyl | e3q9eL1 | A: a/b three-layered sandwiches | X: HAD domain-like | H: HAD domain-related | T: Arginase/deacetylase | F: Hist_deacetyl | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
B | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
C | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
D | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
J | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
K | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
A | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
E | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
F | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
G | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
H | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
I | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
L | 3.40.800.20 | Alpha Beta | 3-Layer(aba) Sandwich | Arginase | Chain A | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00850 | Histone deacetylase domain (Hist_deacetyl) | Histone deacetylase domain | Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyse the removal of the acetyl group. Histone deacetylases are related to other proteins [1]. ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR000286 | Histone deacetylase family | Family | |
IPR023696 | Ureohydrolase domain superfamily | Homologous Superfamily | |
IPR023801 | Histone deacetylase domain | Domain | |
IPR037138 | Histone deacetylase domain superfamily | Homologous Superfamily | |
IPR050284 | Histone deacetylase and polyamine deacetylase | Family |