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1GSJ

Selenomethionine substituted N-acetyl-L-glutamate kinase from Escherichia coli complexed with its substrate n-acetyl-L-glutamate and its substrate analog AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
A0003991molecular_functionacetylglutamate kinase activity
A0004042molecular_functionacetyl-CoA:L-glutamate N-acetyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006526biological_processarginine biosynthetic process
A0006536biological_processglutamate metabolic process
A0006974biological_processDNA damage response
A0008652biological_processamino acid biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0042450biological_processarginine biosynthetic process via ornithine
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A1261
ChainResidue
AASP162
AANP1260
AHOH2133
AHOH2194

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NLG A1259
ChainResidue
ALEU80
AASN158
AVAL159
AALA161
AANP1260
AHOH2194
AHOH2195
AHOH2196
AGLY43
AGLY44
AGLY45
ALEU65
AARG66

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ANP A1260
ChainResidue
ALYS8
AGLY10
AGLY11
AGLY43
AGLY44
AGLY45
AALA161
AASP162
ASER180
AASP181
ALEU186
AILE209
AILE210
ATHR211
AASP212
AMSE214
ALYS217
ANLG1259
AMG1261
AHOH2035
AHOH2197
AHOH2198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12005432, ECO:0000269|PubMed:12875848
ChainResidueDetails
AASN158
AGLY44
AARG66

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:12875848
ChainResidueDetails
AASP181
AILE209

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305|PubMed:12875848
ChainResidueDetails
ALYS8
ALYS217

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

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PDB entries from 2024-04-17

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