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4PS1

Caspase-8 specific unnatural amino acid peptides

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 Residues4
DetailsBINDING SITE FOR RESIDUE DTT A 501
ChainResidue
ATHR337
AGLU396
ATHR469
AHOH669

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DTT B 501
ChainResidue
BTHR337
BGLU396
BTHR469
BHOH632
BHOH643

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DTT C 501
ChainResidue
CTHR337
CGLU396
CTHR469
CHOH626
DHOH743

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DTT D 501
ChainResidue
CHOH680
DTHR337
DGLU396
DTHR469
DHOH647

Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HsnmdCfiCcILSHG
ChainResidueDetails
AHIS304-GLY318

site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKVFFIQACQG
ChainResidueDetails
ALYS351-GLY362

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"evidences":[{"source":"PubMed","id":"10508785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O89110","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"(Microbial infection) ADP-riboxanated arginine","evidences":[{"source":"PubMed","id":"35338844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 818
ChainResidueDetails
AARG258electrostatic stabiliser
AHIS317proton acceptor, proton donor
AGLY318electrostatic stabiliser
ACYS360nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 818
ChainResidueDetails
BARG258electrostatic stabiliser
BHIS317proton acceptor, proton donor
BGLY318electrostatic stabiliser
BCYS360nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA3
Number of Residues4
DetailsM-CSA 818
ChainResidueDetails
CARG258electrostatic stabiliser
CHIS317proton acceptor, proton donor
CGLY318electrostatic stabiliser
CCYS360nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA4
Number of Residues4
DetailsM-CSA 818
ChainResidueDetails
DARG258electrostatic stabiliser
DHIS317proton acceptor, proton donor
DGLY318electrostatic stabiliser
DCYS360nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2025-08-06

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