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2W21

Crystal structure of the aminoacid kinase domain of the glutamate 5 kinase of Escherichia coli.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004349molecular_functionglutamate 5-kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006561biological_processproline biosynthetic process
A0016301molecular_functionkinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1259
ChainResidue
AGLY12
ATHR13
ASER14
AVAL15
ATHR169
AASP170
ALYS217
AHOH2002

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1260
ChainResidue
ASER50
AVAL146
AGLY147
AASP148
AASN149
AASP150
ALYS10

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1261
ChainResidue
ATHR104
AARG105
AALA106
AARG113
ATHR141
AALA142

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1262
ChainResidue
ATHR13
ASER50
AGLY51
AALA52
AILE53
AALA54

Functional Information from PROSITE/UniProt
site_idPS00902
Number of Residues18
DetailsGLUTAMATE_5_KINASE Glutamate 5-kinase signature. SglGtGGMsTKLqAAdvA
ChainResidueDetails
ASER207-ALA224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17321544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J5T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J5V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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