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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7WTD

Cryo-EM structure of human pyruvate carboxylase with acetyl-CoA in the intermediate state 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004736molecular_functionpyruvate carboxylase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006090biological_processpyruvate metabolic process
A0006094biological_processgluconeogenesis
A0006739biological_processNADP+ metabolic process
A0009374molecular_functionbiotin binding
A0010629biological_processnegative regulation of gene expression
A0019074biological_processviral RNA genome packaging
A0019076biological_processviral release from host cell
A0019674biological_processNAD+ metabolic process
A0042802molecular_functionidentical protein binding
A0044794biological_processhost-mediated activation of viral process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004736molecular_functionpyruvate carboxylase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006090biological_processpyruvate metabolic process
B0006094biological_processgluconeogenesis
B0006739biological_processNADP+ metabolic process
B0009374molecular_functionbiotin binding
B0010629biological_processnegative regulation of gene expression
B0019074biological_processviral RNA genome packaging
B0019076biological_processviral release from host cell
B0019674biological_processNAD+ metabolic process
B0042802molecular_functionidentical protein binding
B0044794biological_processhost-mediated activation of viral process
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004736molecular_functionpyruvate carboxylase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005829cellular_componentcytosol
C0006090biological_processpyruvate metabolic process
C0006094biological_processgluconeogenesis
C0006739biological_processNADP+ metabolic process
C0009374molecular_functionbiotin binding
C0010629biological_processnegative regulation of gene expression
C0019074biological_processviral RNA genome packaging
C0019076biological_processviral release from host cell
C0019674biological_processNAD+ metabolic process
C0042802molecular_functionidentical protein binding
C0044794biological_processhost-mediated activation of viral process
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004736molecular_functionpyruvate carboxylase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005829cellular_componentcytosol
D0006090biological_processpyruvate metabolic process
D0006094biological_processgluconeogenesis
D0006739biological_processNADP+ metabolic process
D0009374molecular_functionbiotin binding
D0010629biological_processnegative regulation of gene expression
D0019074biological_processviral RNA genome packaging
D0019076biological_processviral release from host cell
D0019674biological_processNAD+ metabolic process
D0042802molecular_functionidentical protein binding
D0044794biological_processhost-mediated activation of viral process
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00188
Number of Residues18
DetailsBIOTIN Biotin-requiring enzymes attachment site. GQpLcvLsAMKMetvVtS
ChainResidueDetails
AGLY1134-SER1151
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1076
DetailsDomain: {"description":"Pyruvate carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01151","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18297087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"18297087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues50
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q05920","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"18297087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P52873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues900
DetailsDomain: {"description":"Biotin carboxylation"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues394
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues138
DetailsDomain: {"description":"Biotinyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q05920","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q05920","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6548474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7918683","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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