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2JJ4

The complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC7942

Functional Information from GO Data
ChainGOidnamespacecontents
A0003991molecular_functionacetylglutamate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006526biological_processarginine biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0042450biological_processarginine biosynthetic process via ornithine
A0042802molecular_functionidentical protein binding
B0003991molecular_functionacetylglutamate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006526biological_processarginine biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0042450biological_processarginine biosynthetic process via ornithine
B0042802molecular_functionidentical protein binding
C0003991molecular_functionacetylglutamate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006526biological_processarginine biosynthetic process
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0042450biological_processarginine biosynthetic process via ornithine
C0042802molecular_functionidentical protein binding
D0000166molecular_functionnucleotide binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006808biological_processregulation of nitrogen utilization
D0030234molecular_functionenzyme regulator activity
D0042802molecular_functionidentical protein binding
E0000166molecular_functionnucleotide binding
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005829cellular_componentcytosol
E0006808biological_processregulation of nitrogen utilization
E0030234molecular_functionenzyme regulator activity
E0042802molecular_functionidentical protein binding
F0000166molecular_functionnucleotide binding
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005829cellular_componentcytosol
F0006808biological_processregulation of nitrogen utilization
F0030234molecular_functionenzyme regulator activity
F0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NLG A 1292
ChainResidue
AGLY69
AGLY70
AGLY71
AILE74
ALEU91
AARG92
ASER174
AASN185
AALA188

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NLG B 1292
ChainResidue
BGLY69
BGLY70
BGLY71
BILE74
BGLY90
BLEU91
BARG92
BASN185
BALA188

Functional Information from PROSITE/UniProt
site_idPS00496
Number of Residues6
DetailsPII_GLNB_UMP P-II protein uridylation site. YRGSEY
ChainResidueDetails
DTYR46-TYR51

site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgeiGDGKIFVspV
ChainResidueDetails
DTHR83-VAL96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:7592328
ChainResidueDetails
DSER49
ESER49
FSER49
BGLY70
BARG92
BASN185
CGLY70
CARG92
CASN185

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675
ChainResidueDetails
DTYR51
ETYR51
FTYR51
BLYS248
CLYS35
CLYS248

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1oh9
ChainResidueDetails
AGLY38
ALYS35
ALYS248
AGLY71

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1oh9
ChainResidueDetails
BGLY38
BLYS35
BLYS248
BGLY71

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1oh9
ChainResidueDetails
CGLY38
CLYS35
CLYS248
CGLY71

225158

PDB entries from 2024-09-18

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