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2ZCI

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004611molecular_functionphosphoenolpyruvate carboxykinase activity
A0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0016831molecular_functioncarboxy-lyase activity
A0017076molecular_functionpurine nucleotide binding
A0019543biological_processpropionate catabolic process
A0030145molecular_functionmanganese ion binding
A0032869biological_processcellular response to insulin stimulus
A0042594biological_processresponse to starvation
A0046327biological_processglycerol biosynthetic process from pyruvate
A0046872molecular_functionmetal ion binding
A0071333biological_processcellular response to glucose stimulus
A0071549biological_processcellular response to dexamethasone stimulus
B0004611molecular_functionphosphoenolpyruvate carboxykinase activity
B0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0016831molecular_functioncarboxy-lyase activity
B0017076molecular_functionpurine nucleotide binding
B0019543biological_processpropionate catabolic process
B0030145molecular_functionmanganese ion binding
B0032869biological_processcellular response to insulin stimulus
B0042594biological_processresponse to starvation
B0046327biological_processglycerol biosynthetic process from pyruvate
B0046872molecular_functionmetal ion binding
B0071333biological_processcellular response to glucose stimulus
B0071549biological_processcellular response to dexamethasone stimulus
C0004611molecular_functionphosphoenolpyruvate carboxykinase activity
C0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0016831molecular_functioncarboxy-lyase activity
C0017076molecular_functionpurine nucleotide binding
C0019543biological_processpropionate catabolic process
C0030145molecular_functionmanganese ion binding
C0032869biological_processcellular response to insulin stimulus
C0042594biological_processresponse to starvation
C0046327biological_processglycerol biosynthetic process from pyruvate
C0046872molecular_functionmetal ion binding
C0071333biological_processcellular response to glucose stimulus
C0071549biological_processcellular response to dexamethasone stimulus
D0004611molecular_functionphosphoenolpyruvate carboxykinase activity
D0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0016831molecular_functioncarboxy-lyase activity
D0017076molecular_functionpurine nucleotide binding
D0019543biological_processpropionate catabolic process
D0030145molecular_functionmanganese ion binding
D0032869biological_processcellular response to insulin stimulus
D0042594biological_processresponse to starvation
D0046327biological_processglycerol biosynthetic process from pyruvate
D0046872molecular_functionmetal ion binding
D0071333biological_processcellular response to glucose stimulus
D0071549biological_processcellular response to dexamethasone 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
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00452
ChainResidueDetails
ACYS274
BCYS274
CCYS274
DCYS274

site_idSWS_FT_FI2
Number of Residues44
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00452
ChainResidueDetails
AARG82
AARG420
APHE515
BARG82
BTYR221
BLYS230
BHIS250
BSER272
BALA273
BASP297
BASN387
ATYR221
BARG389
BARG420
BPHE515
CARG82
CTYR221
CLYS230
CHIS250
CSER272
CALA273
CASP297
ALYS230
CASN387
CARG389
CARG420
CPHE515
DARG82
DTYR221
DLYS230
DHIS250
DSER272
DALA273
AHIS250
DASP297
DASN387
DARG389
DARG420
DPHE515
ASER272
AALA273
AASP297
AASN387
AARG389

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

219140

PDB entries from 2024-05-01

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