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4WPU

Crystal Structure of E83A mutant of Mtb PEPCK in complex with PEP and GDP

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
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue GDP A 701
ChainResidue
APRO270
ATRP501
APHE502
APHE510
AGLY514
APHE515
AASN518
AHOH817
AHOH876
AHOH1089
AALA272
ACYS273
AGLY274
ALYS275
ATHR276
AASN277
AASP362
AARG420

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 702
ChainResidue
ATHR86
AILE88
ATHR99
AASN100
AASN101
AARG234
ALEU467
APRO468
AHOH1052

site_idAC3
Number of Residues5
Detailsbinding site for residue PEP A 703
ChainResidue
AARG81
AGLY221
AGLY222
AARG389
AHOH962

Functional Information from PROSITE/UniProt
site_idPS00505
Number of Residues9
DetailsPEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN
ChainResidueDetails
APHE269-ASN277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452
ChainResidueDetails
ACYS273

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|Ref.2
ChainResidueDetails
ALYS229
AHIS249
AASP296
AASN387
AARG81

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452
ChainResidueDetails
AALA272
AARG389
AARG420
APHE515
ATYR220
ASER271

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PDB entries from 2024-05-15

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