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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1pau.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)
Bd1pau.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

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.50.1460 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
B3.30.70.1470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits Caspase-likeCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00656Caspase domain (Peptidase_C14)Caspase domain- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
APOPAIN
APOPAIN
ACE-ASP-GLU-VAL-ASJ---

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosP42574
PharosP42574

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
ACE RESIDAA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354

PSI-MOD :  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 RESIDAA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic 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]
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Explore in 3DM-CSA Motif Definition
EC: 3.4.22 (PDB Primary Data)