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4G1P

Structural and Mechanistic Basis of Substrate Recognition by Novel Di-peptidase Dug1p From Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0006508biological_processproteolysis
A0006751biological_processglutathione catabolic process
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008242molecular_functionomega peptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016805molecular_functiondipeptidase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0070573molecular_functionmetallodipeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AASP137
AGLU172
AHIS450
AGLY503

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AASP137
AASP200
AGLY503

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR LINKED RESIDUES A 503 to 504
ChainResidue
AGLU172
ACYS218
AHIS233
ATHR335
AARG348
AHIS385
ASER422
AHIS450
AZN501
AZN502
AHOH632
AASP137
AGLU171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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