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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6G2D

Citrate-induced acetyl-CoA carboxylase (ACC-Cit) filament at 5.4 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003989molecular_functionacetyl-CoA carboxylase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006084biological_processacetyl-CoA metabolic process
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006637biological_processacyl-CoA metabolic process
B0008610biological_processlipid biosynthetic process
B0016874molecular_functionligase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0046949biological_processfatty-acyl-CoA biosynthetic process
B0051289biological_processprotein homotetramerization
B2001295biological_processmalonyl-CoA biosynthetic process
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0003989molecular_functionacetyl-CoA carboxylase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006084biological_processacetyl-CoA metabolic process
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0006637biological_processacyl-CoA metabolic process
C0008610biological_processlipid biosynthetic process
C0016874molecular_functionligase activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0046949biological_processfatty-acyl-CoA biosynthetic process
C0051289biological_processprotein homotetramerization
C2001295biological_processmalonyl-CoA biosynthetic process
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0003989molecular_functionacetyl-CoA carboxylase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0006084biological_processacetyl-CoA metabolic process
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0006637biological_processacyl-CoA metabolic process
D0008610biological_processlipid biosynthetic process
D0016874molecular_functionligase activity
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0046949biological_processfatty-acyl-CoA biosynthetic process
D0051289biological_processprotein homotetramerization
D2001295biological_processmalonyl-CoA biosynthetic process
F0000166molecular_functionnucleotide binding
F0003824molecular_functioncatalytic activity
F0003989molecular_functionacetyl-CoA carboxylase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005739cellular_componentmitochondrion
F0005829cellular_componentcytosol
F0006084biological_processacetyl-CoA metabolic process
F0006629biological_processlipid metabolic process
F0006631biological_processfatty acid metabolic process
F0006633biological_processfatty acid biosynthetic process
F0006637biological_processacyl-CoA metabolic process
F0008610biological_processlipid biosynthetic process
F0016874molecular_functionligase activity
F0042802molecular_functionidentical protein binding
F0046872molecular_functionmetal ion binding
F0046949biological_processfatty-acyl-CoA biosynthetic process
F0051289biological_processprotein homotetramerization
F2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00188
Number of Residues18
DetailsBIOTIN Biotin-requiring enzymes attachment site. GQcYaeIeVMKMvmtLtA
ChainResidueDetails
BGLY776-ALA793
site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASeggGGkG
ChainResidueDetails
BTYR306-GLY320
site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL
ChainResidueDetails
BPHE435-LEU442
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues382
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues148
DetailsDomain: {"description":"Biotinyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues676
DetailsDomain: {"description":"CoA carboxyltransferase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01136","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues632
DetailsDomain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1316
DetailsRegion: {"description":"Carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01138","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"UniProtKB","id":"P11497","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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