Structure of PDB 1od2 Chain B

Receptor sequence
>1od2B (length=695) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PKRYKAHLMGTTYVYDFPELFRQASSSQWKNFSADVKLTDDFFISNELIE
DENGELTEVEREPGANAIGMVAFKITVKTPEYPRGRQFVVVANDITFKIG
SFGPQEDEFFNKVTEYARKRGIPRIYLAANSGARIGMAEEIVPLFQVAWN
DAANPDKGFQYLYLTSEGMETLKKFDKENSVLTERTVINGEERFVIKTII
GSEDGLGVECLRGSGLIAGATSRAYHDIFTITLVTCRSVGIGAYLVRLGQ
RAIQVEGQPIILTGAPAINKMLGREVYTSNLQLGGTQIMYNNGVSHLTAV
DDLAGVEKIVEWMSYVPAKRNMPVPILETKDTWDRPVDFTPTNDETYDVR
WMIEGRETESGFEYGLFDKGSFFETLSGWAKGVVVGRARLGGIPLGVIGV
ETRTVENLIPADPANPNSAETLIQEPGQVWHPNSAFKTAQAINDFNNGEQ
LPMMILANWRGFSGGQRDMFNEVLKYGSFIVDALVDYKQPIIIYIPPTGE
LRGGSWVVVDPTINADQMEMYADVNARAGVLEPQGMVGIKFRREKLLDTM
NRLDDKYRELRSQLSNKSLAPEVHQQISKQLADRERELLPIYGQISLQFA
DLHDRSSRMVAKGVISKELEWTEARRFFFWRLRRRLNEEYLIKRLSHQVG
EASRLEKIARIRSWYPASVDHEDDRQVATWIEENYKTLDDKLKGL
3D structure
PDB1od2 Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
ChainB
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.4.14: biotin carboxylase.
6.4.1.2: acetyl-CoA 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 ACO B G1998 I2033 K2034 L2189 G504 I539 K540 L695
BS02 ADE B I1593 I1629 I99 I135
Gene Ontology
Molecular Function
GO:0003989 acetyl-CoA carboxylase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1od2, PDBe:1od2, PDBj:1od2
PDBsum1od2
PubMed12663926
UniProtQ00955|ACAC_YEAST Acetyl-CoA carboxylase (Gene Name=ACC1)

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