Structure of PDB 1t9c Chain A

Receptor sequence

>1t9cA (length=596) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

MDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFV
LPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPM
VVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAF
EIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSSRAQDEFVMQSINK
AADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSF
DQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPE
ARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPV
KERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHV
IVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPE
SLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFY
EHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLL
EVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

3D structure

PDB

1t9c Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase.

Chain

Resolution

2.34 Å

3D
structure

Catalytic site residues are labeled in the structure
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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 R227 M263 V290 V406 L431 G432 M434 D459 N486 E488 Q489 M491 V492 W495 L517 G522 L523 K556
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	MG	A	D550 N577 E579	D459 N486 E488
BS02	1SM	A	D379 R380 W586	D288 R289 W495	BindingDB: Ki=51nM
BS03	FAD	A	R241 G307 A308 G309 N312 T334 L335 Q336 L352 M354 H355 G374 A375 R376 D378 R380 V381 E407 V408 N412 G425 D426 A427 M502 G520 G521	R157 G216 A217 G218 N221 T243 L244 Q245 L261 M263 H264 G283 A284 R285 D287 R289 V290 E316 V317 N321 G334 D335 A336 M411 G429 G430
BS04	1SM	A	G116 V191 P192 F201 K251	G32 V107 P108 F117 K167	BindingDB: Ki=51nM

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:1t9c, PDBe:1t9c, PDBj:1t9c
PDBsum	1t9c
PubMed	15709745
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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