Structure of PDB 1ozf Chain B Binding Site BS03

Receptor Information
>1ozf Chain B (length=542) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YPVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPV
RHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVA
LGGAVKRADKAKQSMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAAEQ
GRPGSAFVSLPQDVVDGPVSGKVLPAPQMGAAPDDAIDQVAKLIAQAKNP
IFLLGLMASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSRFAGRV
GLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDVLPAYE
ERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQRELLD
RAQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYLYTFRARQ
VMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSMELETAVR
LKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYAESFGAKG
FAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLH
Ligand information
Ligand IDTPP
InChIInChI=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
InChIKeyAYEKOFBPNLCAJY-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N
FormulaC12 H19 N4 O7 P2 S
NameTHIAMINE DIPHOSPHATE
ChEMBLCHEMBL1236376
DrugBank
ZINCZINC000008215517
PDB chain1ozf Chain B Residue 705 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1ozf The Crystal Structures of Klebsiella pneumoniae Acetolactate Synthase with Enzyme-bound Cofactor and with an Unusual Intermediate.
Resolution2.3 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)		G383 S384 F385 Q408 M410 G434 D435 G436 D462 G464 Y465 N466 M467 V468 Y531
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) I32 G34 A35 K36 I37 E57 T80 S121 Q169 L262 E289 M394 Q420 M422 D447 D474 G476 Y477 M479 V480 Q483 Y543
Catalytic site (residue number reindexed from 1) I28 G30 A31 K32 I33 E53 T76 S114 Q162 L252 E279 M382 Q408 M410 D435 D462 G464 Y465 M467 V468 Q471 Y531
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1ozf, PDBe:1ozf, PDBj:1ozf
PDBsum1ozf
PubMed14557277
UniProtP27696|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

[Back to BioLiP]