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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
A0103046molecular_functionalanylglutamate dipeptidase 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
B0103046molecular_functionalanylglutamate dipeptidase 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
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP101
BASP101

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU166
BGLU166

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18550540
ChainResidueDetails
AHIS99
AGLU167
BHIS99
BASP132
BGLU167
AASP132

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: in other chain
ChainResidueDetails
AASP195
AHIS445
BGLU166
BASP195
BARG343
BSER417
BHIS445
AGLU166
AARG343
ASER417

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BHIS228
BTHR330
AHIS228
ATHR330

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for catalytic activity
ChainResidueDetails
AHIS228
BHIS228

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6Q0N1
ChainResidueDetails
ASER58
BSER58

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q96KP4
ChainResidueDetails
ASER299
BSER299

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PDB entries from 2024-06-12

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