Structure of PDB 1lbm Chain A Binding Site BS01

Receptor Information
>1lbm Chain A (length=194) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVRVKICGITNLEDALFSVESGADAVGFVFYPKSKRYISPEDARRISVEL
PPFVFRVGVFVNEEPEKILDVASYVQLNAVQLHGEEPIELCRKIAERILV
IKAVGVSNERDMERALNYREFPILLDTFDWSLILPYRDRFRYLVLSGGLN
PENVRSAIDVVRPFAVDVSSGVEAFPGKKDHDSIKMFIKNAKGL
Ligand information
Ligand ID137
InChIInChI=1S/C12H18NO9P/c14-9(11(16)10(15)6-22-23(19,20)21)5-13-8-4-2-1-3-7(8)12(17)18/h1-4,9-11,13-16H,5-6H2,(H,17,18)(H2,19,20,21)/t9-,10-,11+/m1/s1
InChIKeyAULMJMUNCOBRHC-MXWKQRLJSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)C(O)CNc1ccccc1C(=O)O
OpenEye OEToolkits 1.5.0c1ccc(c(c1)C(=O)O)NC[C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O
CACTVS 3.341O[C@H](CNc1ccccc1C(O)=O)[C@H](O)[C@H](O)CO[P](O)(O)=O
CACTVS 3.341O[CH](CNc1ccccc1C(O)=O)[CH](O)[CH](O)CO[P](O)(O)=O
OpenEye OEToolkits 1.5.0c1ccc(c(c1)C(=O)O)NCC(C(C(COP(=O)(O)O)O)O)O
FormulaC12 H18 N O9 P
Name1-(O-CARBOXY-PHENYLAMINO)-1-DEOXY-D-RIBULOSE-5-PHOSPHATE
ChEMBL
DrugBankDB03543
ZINCZINC000002047810
PDB chain1lbm Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1lbm Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates
Resolution2.8 Å
Binding residue
(original residue number in PDB)		C7 S34 R36 H83 D126 G158 G159 D178 S180 S181
Binding residue
(residue number reindexed from 1)		C7 S34 R36 H83 D126 G147 G148 D167 S169 S170
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) C7 D126
Catalytic site (residue number reindexed from 1) C7 D126
Enzyme Commision number 5.3.1.24: phosphoribosylanthranilate isomerase.
Gene Ontology
Molecular Function
GO:0004640 phosphoribosylanthranilate isomerase activity
GO:0016853 isomerase activity
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1lbm, PDBe:1lbm, PDBj:1lbm
PDBsum1lbm
PubMed12356303
UniProtQ56320|TRPF_THEMA N-(5'-phosphoribosyl)anthranilate isomerase (Gene Name=trpF)

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