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1OS1

Structure of Phosphoenolpyruvate Carboxykinase complexed with ATP,Mg, Ca 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 Residues7
DetailsBINDING SITE FOR RESIDUE MG A 998
ChainResidue
ATHR255
AASP268
ATYR286
AATP541
AHOH674
AHOH716
AHOH738

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 999
ChainResidue
AASP269
AATP541
APYR542
AHOH719
ALYS213
AHIS232

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATP A 541
ChainResidue
ALEU249
ASER250
AGLY251
ATHR252
AGLY253
ALYS254
ATHR255
ATHR256
AASP269
AARG333
AARG449
AILE450
ASER451
AILE452
ATHR455
AHOH674
AHOH716
AHOH719
AHOH738
AHOH754
AMG998
ACA999

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR A 542
ChainResidue
AARG65
ATYR207
ALYS213
ASER250
AGLY393
ACA999

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

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PDB entries from 2025-07-16

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