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2ZCI

Structure of a GTP-dependent bacterial PEP-carboxykinase from Corynebacterium glutamicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004611molecular_functionphosphoenolpyruvate carboxykinase activity
A0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006107biological_processoxaloacetate metabolic process
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0017076molecular_functionpurine nucleotide binding
A0019543biological_processpropionate catabolic process
A0030145molecular_functionmanganese ion binding
A0033993biological_processresponse to lipid
A0042594biological_processresponse to starvation
A0046327biological_processglycerol biosynthetic process from pyruvate
A0046872molecular_functionmetal ion binding
A0071333biological_processcellular response to glucose stimulus
B0000166molecular_functionnucleotide binding
B0004611molecular_functionphosphoenolpyruvate carboxykinase activity
B0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006107biological_processoxaloacetate metabolic process
B0016829molecular_functionlyase activity
B0016831molecular_functioncarboxy-lyase activity
B0017076molecular_functionpurine nucleotide binding
B0019543biological_processpropionate catabolic process
B0030145molecular_functionmanganese ion binding
B0033993biological_processresponse to lipid
B0042594biological_processresponse to starvation
B0046327biological_processglycerol biosynthetic process from pyruvate
B0046872molecular_functionmetal ion binding
B0071333biological_processcellular response to glucose stimulus
C0000166molecular_functionnucleotide binding
C0004611molecular_functionphosphoenolpyruvate carboxykinase activity
C0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006107biological_processoxaloacetate metabolic process
C0016829molecular_functionlyase activity
C0016831molecular_functioncarboxy-lyase activity
C0017076molecular_functionpurine nucleotide binding
C0019543biological_processpropionate catabolic process
C0030145molecular_functionmanganese ion binding
C0033993biological_processresponse to lipid
C0042594biological_processresponse to starvation
C0046327biological_processglycerol biosynthetic process from pyruvate
C0046872molecular_functionmetal ion binding
C0071333biological_processcellular response to glucose stimulus
D0000166molecular_functionnucleotide binding
D0004611molecular_functionphosphoenolpyruvate carboxykinase activity
D0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006107biological_processoxaloacetate metabolic process
D0016829molecular_functionlyase activity
D0016831molecular_functioncarboxy-lyase activity
D0017076molecular_functionpurine nucleotide binding
D0019543biological_processpropionate catabolic process
D0030145molecular_functionmanganese ion binding
D0033993biological_processresponse to lipid
D0042594biological_processresponse to starvation
D0046327biological_processglycerol biosynthetic process from pyruvate
D0046872molecular_functionmetal ion binding
D0071333biological_processcellular response to glucose stimulus
Functional Information from PROSITE/UniProt
site_idPS00505
Number of Residues9
DetailsPEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN
ChainResidueDetails
APHE270-ASN278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00452","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues76
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00452","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
ALYS276
AARG389
AHIS250

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
BLYS276
BARG389
BHIS250

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
CLYS276
CARG389
CHIS250

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
DLYS276
DARG389
DHIS250

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
AARG389
AHIS250

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
BARG389
BHIS250

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
CARG389
CHIS250

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
DARG389
DHIS250

246905

PDB entries from 2025-12-31

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