Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
A0006561biological_processproline biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
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
B0006561biological_processproline biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
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 Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS10
ATHR169
ATHR211
BLYS10
BTHR169
BTHR211

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17321544, ECO:0007744|PDB:2J5T, ECO:0007744|PDB:2J5V
ChainResidueDetails
ASER50
AASP137
AASN149
BSER50
BASP137
BASN149

218853

数据于2024-04-24公开中

PDB statisticsPDBj update infoContact PDBjnumon