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1K3C

Phosphoenolpyruvate carboxykinase in complex with ADP, AlF3 and Pyruvate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004611molecular_functionphosphoenolpyruvate carboxykinase activity
A0004612molecular_functionphosphoenolpyruvate carboxykinase (ATP) activity
A0005509molecular_functioncalcium ion binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0017076molecular_functionpurine nucleotide binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 998
ChainResidue
ATHR255
AADP541
AHOH662
AHOH753
AHOH754
AAF3999

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ADP A 541
ChainResidue
ATHR252
AGLY253
ALYS254
ATHR255
ATHR256
ALYS288
AGLU297
ATHR441
AARG449
AILE450
ASER451
ATHR455
AHOH665
AHOH681
AHOH754
AMG998
AAF3999
ALEU249
ASER250
AGLY251

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AF3 A 999
ChainResidue
ALYS213
AHIS232
ASER250
ALYS254
AASP269
AARG333
AADP541
AHOH662
AMG998

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR A 542
ChainResidue
AARG65
ATYR207
ALYS212
ALYS213
ATYR286
AARG333
AHOH663
AHOH774

Functional Information from PROSITE/UniProt
site_idPS00532
Number of Residues16
DetailsPEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWdDdGVfN
ChainResidueDetails
ALEU265-ASN280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11724534","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12837799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17475535","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8599762","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9406547","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase (PEPCK) complexed with ATP, Mg2+, Mn2+, carbon dioxide and oxaloacetate.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
ALYS254
AARG333
AHIS232

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
AARG333
AHIS232

site_idMCSA1
Number of Residues8
DetailsM-CSA 51
ChainResidueDetails
AARG65electrostatic stabiliser, increase electrophilicity
ALYS213metal ligand
AHIS232electrostatic stabiliser, hydrogen bond donor, metal ligand
ASER250steric role
ALYS254electrostatic stabiliser, hydrogen bond donor
ATHR255metal ligand
AASP269metal ligand
AARG333electrostatic stabiliser, hydrogen bond donor

239803

數據於2025-08-06公開中

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