Structure of PDB 1uys Chain C

Receptor sequence
>1uysC (length=659) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
WLQPKRYKAHLMGTTYVYDFPELFRQASSSQWKNFSADVKLTDDFFISNE
LIEDENGELTEVEREPGANAIGMVAFKITVKTPEYPRGRQFVVVANDITF
KIGSFGPQEDEFFNKVTEYARKRGIPRIYLAANSGARIGMAEEIVPLFQV
AWNDAANPDKGFQYLYLTSEGMETLKKFDKENSVLTERTVINGEERFVIK
TIIGSEDGLGVECLRGSGLIAGATSRAYHDIFTITLVTCRSVGIGAYLVR
LGQRAIQVEGQPIILTGAPAINKMLGREVYTSNLQLGGTQIMYNNGVSHL
TAVDDLAGVEKIVEWMSYVPAKRNMPVPILETKDTWDRPVDFTPTNDETY
DVRWMIEGRETESGFEYGLFDKGSFFETLSGWAKGVVVGRARLGGIPLGV
IGVETRTVENLIPADPANPNSAETLIQEPGQVWHPNSAFKTAQAINDFNN
GEQLPMMILANWRGFSGNEVLKYGSFIVDALVDYKQPIIIYIPPTGELRG
GSWVVVDPTINADQMEMYADVNARAGVLEPQGMVGIKFRREKLLDTMNRL
ELLPIYGQISLQFADLHDRSSRMVAKGVISKELEWTEARRFFFWRLRRRL
NEEYLIKRLSHQVGEASRLEKIARIRSWYPASVDHEDDRQVATWIEENYK
TLDDKLKGL
3D structure
PDB1uys Molecular Basis for the Inhibition of the Carboxyltransferase Domain of Acetyl-Coenzyme-A Carboxylase by Haloxyfop and Diclofop
ChainC
Resolution2.8 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 H1L C W1924 F1956 V1967 L1968 G1971 G1997 G1998 V2002 W433 F465 V470 L471 G474 G500 G501 V505
BS02 H1L C A1627 G1734 I1735 Y1738 A136 G243 I244 Y247
Gene Ontology
Molecular Function
GO:0003989 acetyl-CoA carboxylase activity
GO:0016874 ligase activity

View graph for
Molecular Function
External links
PDB RCSB:1uys, PDBe:1uys, PDBj:1uys
PDBsum1uys
PubMed15079078
UniProtQ00955|ACAC_YEAST Acetyl-CoA carboxylase (Gene Name=ACC1)

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