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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
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP104

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU171

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS102
AASP137
AGLU172
AASP200
AHIS450

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER451

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PDB entries from 2024-11-06

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