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4WIU

Crystal Structure of PEPCK (Rv0211) from Mycobacterium tuberculosis in complex with oxalate and Mn2+

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
A0016829molecular_functionlyase activity
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 Residues5
Detailsbinding site for residue MN A 701
ChainResidue
ALYS229
AHIS249
AASP296
AOXL702
AHOH1376

site_idAC2
Number of Residues6
Detailsbinding site for residue OXL A 702
ChainResidue
AMN701
AHOH1151
AARG81
ALYS229
AHIS249
AARG389

site_idAC3
Number of Residues10
Detailsbinding site for residue GOL A 703
ChainResidue
AGLU83
ATHR86
ATHR99
AASN100
AASN101
AARG234
ALEU467
APRO468
AHOH955
AHOH1094

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
AARG81
ALYS229
AHIS249
AASP296
AASN387

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

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PDB entries from 2024-04-24

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