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2J5V

GLUTAMATE 5-KINASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTAMYL-5-PHOSPHATE AND PYROGLUTAMIC ACID

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0004349molecular_functionglutamate 5-kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0055129biological_processL-proline biosynthetic process
A1901973molecular_functionproline binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0004349molecular_functionglutamate 5-kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0055129biological_processL-proline biosynthetic process
B1901973molecular_functionproline binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A1368
ChainResidue
ALYS10
AGLY12
ALEU168
ASO41371

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A1371
ChainResidue
ALYS217
AMG1368
ARGP1370
AHOH2088
AHOH2089
ALYS10
AGLY12
ATHR13
ASER14
AVAL15

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B1370
ChainResidue
BLYS10
BGLY12
BTHR13
BSER14
BVAL15
BASP170
BLYS217
BRGP1369
BHOH2075

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PCA A1369
ChainResidue
ATHR13
ASER50
AGLY51
AALA52
AILE53
AASN134
ARGP1370

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE RGP A1370
ChainResidue
ALYS10
AGLY12
ATHR13
ASER50
AGLU135
AASP137
ALYS145
AASP148
AASN149
APCA1369
ASO41371

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PCA B1368
ChainResidue
BTHR13
BSER50
BGLY51
BALA52
BILE53
BALA54
BASN134
BASP137
BRGP1369

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE RGP B1369
ChainResidue
BLYS10
BGLY12
BTHR13
BSER50
BGLU135
BASP137
BGLY147
BASP148
BASN149
BASP150
BPCA1368
BSO41370

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 Residues156
DetailsDomain: {"description":"PUA","evidences":[{"source":"HAMAP-Rule","id":"MF_00456","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
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

247536

PDB entries from 2026-01-14

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