1PAU
Crystal structure of the complex of apopain with the tetrapeptide aldehyde inhibitor AC-DEVD-CHO
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | d1pau.1 | Alpha and beta proteins (a/b) | Caspase-like | Caspase-like | Caspase catalytic domain | Apopain (caspase-3, cpp32) | human (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
B | d1pau.1 | Alpha and beta proteins (a/b) | Caspase-like | Caspase-like | Caspase catalytic domain | Apopain (caspase-3, cpp32) | human (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.40.50.1460 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | CATH (4.3.0) | |
B | 3.30.70.1470 | Alpha Beta | 2-Layer Sandwich | Alpha-Beta Plaits | Caspase-like | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00656 | Caspase domain (Peptidase_C14) | Caspase domain | - | Domain | |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR029030 | Caspase-like domain superfamily | Homologous Superfamily | |
IPR001309 | Peptidase C14, p20 domain | Domain | |
IPR011600 | Peptidase C14, caspase domain | Domain | |
IPR016129 | Peptidase family C14A, His active site | Active Site | |
IPR015917 | Peptidase C14A, caspase catalytic domain | Domain | |
IPR033139 | Peptidase family C14A, cysteine active site | Active Site | |
IPR002138 | Peptidase C14, caspase non-catalytic subunit p10 | Domain | |
IPR029030 | Caspase-like domain superfamily | Homologous Superfamily | |
IPR001309 | Peptidase C14, p20 domain | Domain | |
IPR011600 | Peptidase C14, caspase domain | Domain | |
IPR016129 | Peptidase family C14A, His active site | Active Site | |
IPR015917 | Peptidase C14A, caspase catalytic domain | Domain | |
IPR033139 | Peptidase family C14A, cysteine active site | Active Site | |
IPR002138 | Peptidase C14, caspase non-catalytic subunit p10 | Domain |
Pharos: Disease Associations Pharos Homepage Annotation
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
ACE | AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 :  N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 | :  |
ASJ | AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 | : 
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
caspase-3 M-CSA #815 | Caspase-3 from Homo sapiens is a member of a family of intracellular cysteine proteases that cleave substrates specifically at an aspartic acid residue. Caspases share a high degree of homology, not only within caspases from the same species but also across various species. Caspases control the proteolytic cascade central to the initiation and regulation of apoptosis. Caspase-3 is known as the executioner protease. The inactive form of caspase-3 is procaspase-3. This is activated when the procaspase is cleaved at an aspartate residue in the subunit linker, followed by one or more cleavages that remove the pro-domain. | Defined by 5 residues: THR:A-34 [auth A-177]SER:A-35 [auth A-178]HIS:A-93 [auth A-237]GLY:A-94 [auth A-238]CYS:A-135 [auth A-285] | EC: 3.4.22 (PDB Primary Data) EC: 3.4.22.56 (UniProt) |