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2ZOG

Crystal structure of mouse carnosinase CN2 complexed with ZN and bestatin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0016805molecular_functiondipeptidase activity
A0046872molecular_functionmetal ion binding
A0070573molecular_functionmetallodipeptidase activity
B0004180molecular_functioncarboxypeptidase activity
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0016805molecular_functiondipeptidase activity
B0046872molecular_functionmetal ion binding
B0070573molecular_functionmetallodipeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 2001
ChainResidue
AASP132
AGLU167
AHIS445

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2002
ChainResidue
AHIS99
AASP132
AGLU166
AASP195

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 3001
ChainResidue
BHIS445
BASP132
BGLU167

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 3002
ChainResidue
BHIS99
BASP132
BASP195

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE BES A 1080
ChainResidue
AHIS99
AASP132
AGLU166
AGLU167
AASP195
ATYR197
AARG343
AGLU414
ASER417
AHIS445
BHIS228
BTHR330

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE BES B 1081
ChainResidue
AHIS228
ATHR330
BHIS99
BASP132
BGLU166
BGLU167
BASP195
BTYR197
BARG343
BGLU414
BSER417
BHIS445

Functional Information from PROSITE/UniProt
site_idPS00759
Number of Residues40
DetailsARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. STDdKGpvAgwMnaleayqktgqeipvn.LrFCLegMEEsG
ChainResidueDetails
ASER130-GLY169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18550540","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"description":"in other chain"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6Q0N1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q96KP4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
AGLU166

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
BGLU166

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PDB entries from 2025-07-23

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