Structure of PDB 1lbm Chain A

Receptor sequence
>1lbmA (length=194) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MVRVKICGITNLEDALFSVESGADAVGFVFYPKSKRYISPEDARRISVEL
PPFVFRVGVFVNEEPEKILDVASYVQLNAVQLHGEEPIELCRKIAERILV
IKAVGVSNERDMERALNYREFPILLDTFDWSLILPYRDRFRYLVLSGGLN
PENVRSAIDVVRPFAVDVSSGVEAFPGKKDHDSIKMFIKNAKGL
3D structure
PDB1lbm Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 137 A C7 S34 R36 H83 D126 G158 G159 D178 S180 S181 C7 S34 R36 H83 D126 G147 G148 D167 S169 S170
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

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Molecular Function
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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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