Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8WRA

The Crystal Structure of CASP1 from Biortus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. MPTSSGSEGnVK
ChainResidueDetails
AMET123-LYS134

site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HktsdStfLvFMSHG
ChainResidueDetails
AHIS224-GLY238

site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKVIIIQACRG
ChainResidueDetails
ALYS276-GLY287

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"1574116","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"1574116","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32051255","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"30065070","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 718
ChainResidueDetails
AHIS237proton acceptor, proton donor
AGLY238electrostatic stabiliser
ACYS285nucleofuge, nucleophile, proton acceptor, proton donor
AARG286electrostatic stabiliser
AGLU390electrostatic stabiliser

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon