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1LFW

Crystal structure of pepV

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016805molecular_functiondipeptidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AASP119
AGLU154
AHIS439
AAEP683

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1002
ChainResidue
AHIS87
AASP119
AASP177
AAEP683

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AEP A 683
ChainResidue
AASP119
AGLU153
AGLU154
AASP177
AASN217
AHIS269
AARG350
AGLY414
AGLY415
AMET438
AHIS439
AZN1001
AZN1002
AHOH1164
AHOH1512
AHIS87

Functional Information from PROSITE/UniProt
site_idPS00758
Number of Residues10
DetailsARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. LGIIGHmDVV
ChainResidueDetails
ALEU82-VAL91

site_idPS00759
Number of Residues40
DetailsARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. SADdKGpsLtaYygmlllkeagfkpkkk.IdFVLgtNEEtN
ChainResidueDetails
ASER117-ASN156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP89

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AGLU153

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:12176387
ChainResidueDetails
AHIS87
AASP119
AGLU154
AASP177
AHIS439

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AARG350

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
AGLU153

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PDB entries from 2024-07-10

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