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5I67

Crystal Structure Analysis of MTB PEPCK mutant C273S

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 Residues19
Detailsbinding site for residue GDP A 701
ChainResidue
APRO270
AARG376
ATRP500
APHE501
APHE509
AGLY513
APHE514
AASN517
AMN706
AHOH821
AHOH826
ASER271
AALA272
AGLY274
ALYS275
ATHR276
AASN277
AASP361
APHE375

site_idAC2
Number of Residues4
Detailsbinding site for residue PEG A 702
ChainResidue
AARG301
ATYR308
AVAL310
AGLN407

site_idAC3
Number of Residues3
Detailsbinding site for residue PEG A 703
ChainResidue
AARG157
ATHR158
AASN339

site_idAC4
Number of Residues5
Detailsbinding site for residue PEG A 704
ChainResidue
APRO283
ATHR284
AILE285
AGLY287
ATRP288

site_idAC5
Number of Residues4
Detailsbinding site for residue MN A 705
ChainResidue
ALYS229
AHIS249
AASP296
AHOH835

site_idAC6
Number of Residues5
Detailsbinding site for residue MN A 706
ChainResidue
ATHR276
AGDP701
AHOH815
AHOH821
AHOH834

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
ASER273

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|Ref.2
ChainResidueDetails
AARG81
ALYS229
AHIS249
AASP296
AASN386

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452
ChainResidueDetails
ATYR220
ASER271
AALA272
AARG388
AARG419
APHE514

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PDB entries from 2024-09-04

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