Structure of PDB 2f9y Chain B

Receptor sequence
>2f9yB (length=257) Species: 562 (Escherichia coli) [Search protein sequence]
VWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMTARNRLHSLLDEGSLVE
LGSELEPKDVLKFRDSKKYKQKETGEKDALVVMKGTLYGMPVVAAAFEFA
FMGGSMGSVVGARFVRAVEQALEDNCPLICFSASGGARMQEALMSLMQMA
KTSAALAKMQERGLPYISVLTDPTMGGVSASFAMLGDLNIAEPKALIGFA
GPRVIEQTVREKLPPGFQRSEFLIEKGAIDMIVRRPEMRLKLASILAKLM
NLPAPNP
3D structure
PDB2f9y The Structure of the Carboxyltransferase Component of Acetyl-CoA Carboxylase Reveals a Zinc-Binding Motif Unique to the Bacterial Enzyme(,).
ChainB
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G204 G205
Catalytic site (residue number reindexed from 1) G176 G177
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 C30 C49 C8 C27
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0003989 acetyl-CoA carboxylase activity
GO:0005515 protein binding
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:0006417 regulation of translation
GO:0006633 fatty acid biosynthetic process
GO:0017148 negative regulation of translation
GO:0042759 long-chain fatty acid biosynthetic process
GO:2001295 malonyl-CoA biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009317 acetyl-CoA carboxylase complex
GO:0009329 acetate CoA-transferase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2f9y, PDBe:2f9y, PDBj:2f9y
PDBsum2f9y
PubMed16460018
UniProtP0A9Q5|ACCD_ECOLI Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (Gene Name=accD)

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