Structure of PDB 2f9i Chain B

Receptor sequence
>2f9iB (length=260) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
PAGIMTKCPKCKKIMYTKELAENLNVCFNCDHHIALTAYKRIEAISDEGS
FTEFDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDGMKFGV
AVMDSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGII
SLMQMGKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPK
ALIGFAGRRVIEQTINEKLPDDFQTAEFLLEHGQLDKVVHRNDMRQTLSE
ILKIHQEVTK
3D structure
PDB2f9i The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.
ChainB
Resolution1.98 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G207 G208
Catalytic site (residue number reindexed from 1) G182 G183
Enzyme Commision number 2.1.3.15: acetyl-CoA carboxytransferase.
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 ZN B C33 C36 C52 C55 C8 C11 C27 C30
Gene Ontology
Molecular Function
GO:0003989 acetyl-CoA carboxylase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0016743 carboxyl- or carbamoyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:2001295 malonyl-CoA biosynthetic process
Cellular Component
GO:0005737 cytoplasm
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:2f9i, PDBe:2f9i, PDBj:2f9i
PDBsum2f9i
PubMed16460018
UniProtQ5HF73|ACCD_STAAC Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (Gene Name=accD)

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