Structure of PDB 1dv1 Chain A

Receptor sequence

>1dv1A (length=433) Species: 562 (Escherichia coli)

LDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCI
GPAPSVKSYLNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFI
FIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKR
IGYPVIIKASMRVVRGDAELAQSISMTRAEANDMVYMEKYLENPRHVEIQ
VLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKA
CVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQL
RIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGF
GVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDG
IKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGL

3D structure

• PDB: 1dv1 Movement of the biotin carboxylase B-domain as a result of ATP binding.
• Chain: A
• Resolution: 1.9 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	PO4	A	K238 R292 Q294 V295 E296 R338	K225 R279 Q281 V282 E283 R325

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

External links

• PDB: RCSB:1dv1, PDBe:1dv1, PDBj:1dv1
• PDBsum: 1dv1
• PubMed: 10821865
• UniProt: P24182|ACCC_ECOLI Biotin carboxylase (Gene Name=accC)