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4WL8

Crystal Structure of Mtb PEPCK in complex with non-hydrolyzable analog of GTP

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
A0033993biological_processresponse to lipid
A0042594biological_processresponse to starvation
A0046327biological_processglycerol biosynthetic process from pyruvate
A0046872molecular_functionmetal ion binding
A0071333biological_processcellular response to glucose stimulus
Functional Information from PDB Data
site_idAC1
Number of Residues26
Detailsbinding site for residue GNP A 701
ChainResidue
APRO270
AARG377
AARG420
ATRP501
APHE502
APHE510
AGLY514
APHE515
AASN518
AMN703
AHOH801
ASER271
AHOH810
AHOH852
AHOH882
AHOH897
AHOH1003
AHOH1072
AHOH1423
AALA272
ACYS273
AGLY274
ALYS275
ATHR276
AASN277
AASP362

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 702
ChainResidue
ATHR86
ATHR99
AASN100
AASN101
AARG234
ALEU467
APRO468
AHOH1394

site_idAC3
Number of Residues6
Detailsbinding site for residue MN A 703
ChainResidue
ATHR276
AGNP701
AHOH801
AHOH810
AHOH1383
AHOH1400

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 2024-10-02

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