Structure of PDB 6lpi Chain A Binding Site BS04

Receptor Information
>6lpi Chain A (length=531) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHE
QGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIADARLDSIPLICITG
QVPASEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWI
DIPKDVQTAVFEIQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGG
GVINAPARVRELAEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTN
YILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPH
VAIQADVDDVLAQLIPLVEAQPRAEWHQLVADLQREFPCPPLSHYGLINA
VAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAA
IGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGL
VHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNDPQASLQEIIN
RPGPALIHVRIDAEEKVYPMVPPGAANTEMV
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 chain6lpi Chain C Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6lpi Molecular architecture of the acetohydroxyacid synthase holoenzyme.
Resolution2.849 Å
Binding residue
(original residue number in PDB)		E60 C83 P86
Binding residue
(residue number reindexed from 1)		E50 C73 P76
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) I34 G36 G37 S38 I39 E60 C83 E124 K172 M263 A290 V391 G417 M419 D444 N471 A473 L474 L476 V477 Q480
Catalytic site (residue number reindexed from 1) I24 G26 G27 S28 I29 E50 C73 E106 K154 M243 A270 V365 G391 M393 D418 N445 A447 L448 L450 V451 Q454
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:0005515 protein binding
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: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:6lpi, PDBe:6lpi, PDBj:6lpi
PDBsum6lpi
PubMed32538427
UniProtP08142|ILVB_ECOLI Acetolactate synthase isozyme 1 large subunit (Gene Name=ilvB)

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