Structure of PDB 1dv1 Chain A Binding Site BS01

Receptor Information
>1dv1 Chain A (length=433) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCI
GPAPSVKSYLNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFI
FIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKR
IGYPVIIKASMRVVRGDAELAQSISMTRAEANDMVYMEKYLENPRHVEIQ
VLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKA
CVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQL
RIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGF
GVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDG
IKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGL
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1dv1 Chain A Residue 1000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1dv1 Movement of the biotin carboxylase B-domain as a result of ATP binding.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		K238 R292 Q294 V295 E296 R338
Binding residue
(residue number reindexed from 1)		K225 R279 Q281 V282 E283 R325
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K116 K159 D196 H209 R235 T274 E276 E288 N290 R292 E296 R338
Catalytic site (residue number reindexed from 1) K115 K158 D183 H196 R222 T261 E263 E275 N277 R279 E283 R325
Enzyme Commision number 6.3.4.14: biotin carboxylase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003989 acetyl-CoA carboxylase activity
GO:0004075 biotin carboxylase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0045717 negative regulation of fatty acid biosynthetic process
GO:2001295 malonyl-CoA biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009317 acetyl-CoA carboxylase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dv1, PDBe:1dv1, PDBj:1dv1
PDBsum1dv1
PubMed10821865
UniProtP24182|ACCC_ECOLI Biotin carboxylase (Gene Name=accC)

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