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2X2W

Acetylglutamate kinase from Escherichia coli bound to N-acetyl-L-glutamyl-5-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003991molecular_functionacetylglutamate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006526biological_processL-arginine biosynthetic process
A0006974biological_processDNA damage response
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
B0006974biological_processDNA damage response
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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1260
ChainResidue
AGLY10
AGLY11
AVAL12
ASER180
ALYS217
AX2W1259

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 1260
ChainResidue
BASP181
BLYS217
BHOH2066
BHOH2091
BHOH2092
BGLY11
BVAL12
BSER180

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE X2W A 1259
ChainResidue
ALYS8
ALEU9
AGLY10
AGLY11
AGLY43
AGLY44
AGLY45
AARG66
AASN158
AALA161
ASO41260
AHOH2065

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE X2W B 1259
ChainResidue
BLYS8
BGLY10
BGLY11
BGLY43
BGLY44
BGLY45
BLEU65
BARG66
BASN158
BALA161
BHOH2089
BHOH2090

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12005432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12875848","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12875848","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12875848","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 870
ChainResidueDetails
ALYS8transition state stabiliser
AGLY11transition state stabiliser
AGLY45transition state stabiliser
AASP162activator, steric role
ALYS217transition state stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 870
ChainResidueDetails
BLYS8transition state stabiliser
BGLY11transition state stabiliser
BGLY45transition state stabiliser
BASP162activator, steric role
BLYS217transition state stabiliser

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PDB entries from 2025-12-24

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