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3R5J

Crystal structure of active caspase-2 bound with Ac-ADVAD-CHO

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
C0004197molecular_functioncysteine-type endopeptidase activity
C0006508biological_processproteolysis
C0008234molecular_functioncysteine-type peptidase activity
D0004197molecular_functioncysteine-type endopeptidase activity
D0006508biological_processproteolysis
D0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR CHAIN E OF PEPTIDE (ACE)ADVAD-CHO
ChainResidue
AARG219
BTHR380
BTRP385
BGLY419
BTYR420
BALA421
BPHE426
AHIS277
AGLY278
AGLN318
ACYS320
BALA376
BMET377
BARG378
BASN379

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR CHAIN F OF PEPTIDE (ACE)ADVAD-CHO
ChainResidue
BASP416
CARG219
CHIS277
CGLY278
CGLN318
CCYS320
DALA376
DMET377
DARG378
DASN379
DTHR380
DLYS381
DTRP385
DGLY419
DTYR420
DALA421
DPHE426

Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HrvtdSciVaLLSHG
ChainResidueDetails
AHIS264-GLY278

site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKMFFIQACRG
ChainResidueDetails
ALYS311-GLY322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS277
ACYS320
CHIS277
CCYS320

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PDB entries from 2024-11-06

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