Structure of PDB 1ozf Chain A Binding Site BS03

Receptor Information

>1ozf Chain A (length=545) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

VRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPVRH
EANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVALG
GAVKRADKAKQVHQSMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAAE
QGRPGSAFVSLPQDVVDGPVSGKVLPAPQMGAAPDDAIDQVAKLIAQAKN
PIFLLGLMASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSRFAGR
VGLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDVLPAY
EERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQRELL
DRRGAQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYLYTFR
ARQVMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSMELET
AVRLKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYAESFG
AKGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLH

Ligand information

Ligand ID

TPP

InChI

InChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1

InChIKey

AYEKOFBPNLCAJY-UHFFFAOYSA-O

SMILES

Software	SMILES
CACTVS 3.341	Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0	Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0	Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.341	Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
ACDLabs 10.04	O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N

Formula

C12 H19 N4 O7 P2 S

Name

THIAMINE DIPHOSPHATE

PDB chain

1ozf Chain A Residue 700 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1ozf The Crystal Structures of Klebsiella pneumoniae Acetolactate Synthase with Enzyme-bound Cofactor and with an Unusual Intermediate.
Resolution	2.3 Å
Binding residue (original residue number in PDB)	G395 S396 F397 Q420 M422 G446 D447 G448 D474 G476 Y477 N478 M479 V480 Y543
Binding residue (residue number reindexed from 1)	G386 S387 F388 Q411 M413 G437 D438 G439 D465 G467 Y468 N469 M470 V471 Y534
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	I32 G34 A35 K36 I37 E57 T80 H119 Q120 S121 Q169 L262 E289 M394 Q420 M422 D447 D474 G476 Y477 M479 V480 Q483 Y543
Catalytic site (residue number reindexed from 1)	I26 G28 A29 K30 I31 E51 T74 H113 Q114 S115 Q163 L253 E280 M385 Q411 M413 D438 D465 G467 Y468 M470 V471 Q474 Y534
Enzyme Commision number	2.2.1.6: acetolactate synthase.

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:0009097	isoleucine biosynthetic process
GO:0009099	L-valine biosynthetic process
GO:0019752	carboxylic acid metabolic process
GO:0034077	butanediol metabolic process

	Cellular Component
GO:0005948	acetolactate synthase complex

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1ozf, PDBe:1ozf, PDBj:1ozf
PDBsum	1ozf
PubMed	14557277
UniProt	P27696\|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

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