Structure of PDB 5wdg Chain A Binding Site BS04

Receptor Information
>5wdg Chain A (length=538) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPVR
HEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVAL
GGAVKRADKMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAAEQGRPGS
AFVSLPQDVVDGPVSGKVLPAQMGAAPDDAIDQVAKLIAQAKNPIFLLGL
MASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSRFAGRVGLFNNQ
AGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDVLPAYEERNYTP
DVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQRELLDRRGAQL
NQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYLYSFRARQVMIS
NGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSMELETAVRLKAN
VLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYAESFGAKGFAVE
SAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLH
Ligand information
Ligand IDA4Y
InChIInChI=1S/C17H28N4O11P2S/c1-9-12(5-6-31-34(29,30)32-33(26,27)28)35-17(16(4,25)15(3,24)14(22)23)20-13-11(8-21(9)17)7-18-10(2)19-13/h7,9,12,24-25H,5-6,8H2,1-4H3,(H,22,23)(H,29,30)(H,18,19,20)(H2,26,27,28)/t9-,12+,15+,16-,17-/m0/s1
InChIKeyAMCOUTJLRZHMEE-PLEBXABZSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01C(CC3C(N2Cc1cnc(C)nc1NC2(C(O)(C(O)(C(O)=O)C)C)S3)C)OP(O)(=O)OP(O)(O)=O
OpenEye OEToolkits 2.0.6Cc1ncc2c(n1)NC3(N(C2)C(C(S3)CCOP(=O)(O)OP(=O)(O)O)C)C(C)(C(C)(C(=O)O)O)O
CACTVS 3.385C[CH]1[CH](CCO[P](O)(=O)O[P](O)(O)=O)S[C]2(Nc3nc(C)ncc3CN12)[C](C)(O)[C](C)(O)C(O)=O
OpenEye OEToolkits 2.0.6Cc1ncc2c(n1)N[C@]3(N(C2)[C@H]([C@H](S3)CCOP(=O)(O)OP(=O)(O)O)C)[C@](C)([C@@](C)(C(=O)O)O)O
CACTVS 3.385C[C@H]1[C@@H](CCO[P](O)(=O)O[P](O)(O)=O)S[C@]2(Nc3nc(C)ncc3CN12)[C@@](C)(O)[C@](C)(O)C(O)=O
FormulaC17 H28 N4 O11 P2 S
Name(2S,3S)-2,3-dihydroxy-3-[(7S,8R,9aS)-8-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2,7-dimethyl-5,7,8,10-tetrahydro-9aH-pyrimido[4,5-d][1,3]thiazolo[3,2-a]pyrimidin-9a-yl]-2-methylbutanoic acid
ChEMBL
DrugBank
ZINC
PDB chain5wdg Chain A Residue 605 [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]
PDB5wdg Acetolactate Synthase from Klebsiella pneumoniae in Complex with Mechanism-Based Inhibitor
Resolution2.12 Å
Binding residue
(original residue number in PDB)		M394 S396 F397 Q420 M422 G446 D447 G448 G449 D474 G476 Y477 N478 M479 V480 Y543
Binding residue
(residue number reindexed from 1)		M378 S380 F381 Q404 M406 G430 D431 G432 G433 D458 G460 Y461 N462 M463 V464 Y527
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) I32 G34 A35 K36 I37 E57 T80 Q169 L262 E289 M394 Q420 M422 D447 D474 G476 Y477 M479 V480 Q483 Y543
Catalytic site (residue number reindexed from 1) I27 G29 A30 K31 I32 E52 T75 Q157 L246 E273 M378 Q404 M406 D431 D458 G460 Y461 M463 V464 Q467 Y527
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:5wdg, PDBe:5wdg, PDBj:5wdg
PDBsum5wdg
PubMed
UniProtP27696|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

[Back to BioLiP]