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3T7B

Crystal Structure of N-acetyl-L-glutamate kinase from Yersinia pestis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003991molecular_functionacetylglutamate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006526biological_processL-arginine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0042450biological_processL-arginine biosynthetic process via ornithine
B0000166molecular_functionnucleotide binding
B0003991molecular_functionacetylglutamate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006526biological_processL-arginine biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0042450biological_processL-arginine biosynthetic process via ornithine
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GLU A 258
ChainResidue
ALYS7
AGLY10
AGLY42
AGLY43
AALA160

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GLU B 258
ChainResidue
BALA160
BGLY43
BARG65
BASN157
BASN159

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SRT B 259
ChainResidue
BSER15
BSER15
BGLU16
BGLU16
BGLU17
BGLU17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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