Structure of PDB 5d6r Chain M Binding Site BS03

Receptor Information
>5d6r Chain M (length=553) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PRGSHMDKQYPVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLL
DSSIRIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATA
NSEGDPVVALGGAVKRADKAKQVHQSMDTVAMFSPVTKYAIEVTAPDALA
EVVSNAFRAAEQGRPGSAFVSLPQDVVDGPVSGKVLPASGAPQMGAAPDD
AIDQVAKLIAQAKNPIFLLGLMASQPENSKALRRLLETSHIPVTSTYQAA
GAVNQDNFSRFAGRVGLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNS
GNATLVHIDVLPAYEERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQA
AEILRDRQHQRELQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWI
ARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFL
QSSMELETAVRLKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDF
KAYAESFGAKGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMG
QLH
Ligand information
Ligand IDEN0
InChIInChI=1S/C14H20FN4O11P3S/c1-7-10(3-4-29-33(27,28)30-32(24,25)26)34-14(11(20)12(15)31(21,22)23)19(7)6-9-5-17-8(2)18-13(9)16/h5H,3-4,6H2,1-2H3,(H7-,16,17,18,20,21,22,23,24,25,26,27,28)/p+1
InChIKeyPVRNEYSMVSDDAI-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.385Cc1ncc(C[n+]2c(C)c(CCO[P](O)(=O)O[P](O)(O)=O)sc2C(O)=C(F)[P](O)(O)=O)c(N)n1
ACDLabs 12.01Cc2ncc(C[n+]1c(c(sc1/C(O)=C(\F)P(O)(O)=O)CCOP(=O)(O)OP(O)(=O)O)C)c(n2)N
OpenEye OEToolkits 1.9.2Cc1c(sc([n+]1Cc2cnc(nc2N)C)/C(=C(\F)/P(=O)(O)O)/O)CCOP(=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.9.2Cc1c(sc([n+]1Cc2cnc(nc2N)C)C(=C(F)P(=O)(O)O)O)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.385Cc1ncc(C[n+]2c(C)c(CCO[P](O)(=O)O[P](O)(O)=O)sc2\C(O)=C(/F)[P](O)(O)=O)c(N)n1
FormulaC14 H21 F N4 O11 P3 S
Name3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(Z)-2-fluoro-1-hydroxy-2-phosphonoethenyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium
ChEMBL
DrugBank
ZINC
PDB chain5d6r Chain M Residue 604 [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]
PDB5d6r Acetolactate Synthase from Klebsiella pneumoniae in Complex with Mechanism-Based Inhibitor
Resolution2.276 Å
Binding residue
(original residue number in PDB)		M394 G395 S396 F397 Q420 M422 D447 G448 G449 G476 Y477 N478 M479 V480 Y543
Binding residue
(residue number reindexed from 1)		M393 G394 S395 F396 Q419 M421 D446 G447 G448 G475 Y476 N477 M478 V479 Y542
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G34 I37 E57 H119 Q120 S121 Q169 E289 Q420 D447 D474 G476 Y477 M479 V480 Q483 Y543
Catalytic site (residue number reindexed from 1) G39 I42 E62 H124 Q125 S126 Q174 E294 Q419 D446 D473 G475 Y476 M478 V479 Q482 Y542
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:5d6r, PDBe:5d6r, PDBj:5d6r
PDBsum5d6r
PubMed
UniProtP27696|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

[Back to BioLiP]