Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2W6Z

Crystal structure of Biotin carboxylase from E. coli in complex with the 3-(3-Methyl-but-2-enyl)-3H-purin-6-ylamine fragment

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003989molecular_functionacetyl-CoA carboxylase activity
A0004075molecular_functionbiotin carboxylase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0009317cellular_componentacetyl-CoA carboxylase complex
A0016874molecular_functionligase activity
A0042803molecular_functionprotein homodimerization activity
A0045717biological_processnegative regulation of fatty acid biosynthetic process
A0046872molecular_functionmetal ion binding
A2001295biological_processmalonyl-CoA biosynthetic process
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003989molecular_functionacetyl-CoA carboxylase activity
B0004075molecular_functionbiotin carboxylase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0009317cellular_componentacetyl-CoA carboxylase complex
B0016874molecular_functionligase activity
B0042803molecular_functionprotein homodimerization activity
B0045717biological_processnegative regulation of fatty acid biosynthetic process
B0046872molecular_functionmetal ion binding
B2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE L21 A 1447
ChainResidue
AILE157
ALYS159
AGLU201
ALYS202
ATYR203
ALEU204
ALEU278
AILE437
AHIS438

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1448
ChainResidue
AARG292
AGLN294
AVAL295
AHOH2200

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1446
ChainResidue
BARG292
BGLN294
BVAL295
BHOH2124

Functional Information from PROSITE/UniProt
site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVIIKASgggGGrG
ChainResidueDetails
ATYR154-GLY168

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRI
ChainResidueDetails
APHE286-ILE293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues888
DetailsDomain: {"description":"Biotin carboxylation"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues394
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon