Structure of PDB 1t9b Chain B

Receptor sequence

>1t9bB (length=595) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

MDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFV
LPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPM
VVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAF
EIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSRAQDEFVMQSINKA
ADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFD
QEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEA
RRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVK
ERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVI
VTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPES
LVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYE
HRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLE
VEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

3D structure

PDB

1t9b Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase.

Chain

Resolution

2.2 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	Y113 G115 G116 A117 I118 E139 T162 F201 Q202 E203 K251 R318 M354 V381 V497 L522 G523 M525 D550 N577 E579 Q580 M582 V583 W586 L608 G613 L614 K647
Catalytic site (residue number reindexed from 1)	Y29 G31 G32 A33 I34 E55 T78 F117 Q118 E119 K167 R226 M262 V289 V405 L430 G431 M433 D458 N485 E487 Q488 M490 V491 W494 L516 G521 L522 K555
Enzyme Commision number	2.2.1.6: acetolactate synthase.

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	1CS	B	V191 P192	V107 P108	MOAD: Ki=127nM BindingDB: Ki=127nM
BS02	MG	B	D550 N577 E579	D458 N485 E487
BS03	1CS	B	D379 R380 M582 W586	D287 R288 M490 W494	MOAD: Ki=127nM BindingDB: Ki=127nM
BS04	FAD	B	R241 G307 A308 G309 N312 T334 L335 Q336 M351 L352 M354 H355 G374 A375 R376 D378 R380 V381 E407 V408 N412 G425 D426 A427 Q501 M502 G520 G521	R157 G215 A216 G217 N220 T242 L243 Q244 M259 L260 M262 H263 G282 A283 R284 D286 R288 V289 E315 V316 N320 G333 D334 A335 Q409 M410 G428 G429

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0003984	acetolactate synthase activity
GO:0016740	transferase activity
GO:0030976	thiamine pyrophosphate binding
GO:0046872	metal ion binding
GO:0050660	flavin adenine dinucleotide binding

	Biological Process
GO:0008652	amino acid biosynthetic process
GO:0009082	branched-chain amino acid biosynthetic process
GO:0009097	isoleucine biosynthetic process
GO:0009099	L-valine biosynthetic process

	Cellular Component
GO:0005739	mitochondrion
GO:0005948	acetolactate synthase complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1t9b, PDBe:1t9b, PDBj:1t9b
PDBsum	1t9b
PubMed	15709745
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

[Back to BioLiP]