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6KMT

P32 of caspase-11 mutant C254A

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 PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HqtsdStfLvLMSHG
ChainResidueDetails
AHIS193-GLY207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P29466
ChainResidueDetails
AHIS206
BHIS206
CHIS206
DHIS206

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P49662
ChainResidueDetails
AALA254
BALA254
CALA254
DALA254

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:30135078
ChainResidueDetails
AASP285
BASP285
CASP285
DASP285

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:34671164
ChainResidueDetails
AARG310
BARG310
CARG310
DARG310

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PDB entries from 2024-07-24

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