Structure of PDB 2y85 Chain B

Receptor sequence
>2y85B (length=236) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
MPLILLPAVDVVEGRAVRLVTEYGSAVDAALGWQRDGAEWIHLVDLDAAF
GRGSNHELLAEVVGKLDVQVELSGGIRDDESLAAALATGCARVNVGTAAL
ENPQWCARVIGEHGDQVAVGLDVQIIDGEHRLRGRGWETDGGDLWDVLER
LDSEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDD
LRAIATLTHRGVEGAIVGKALYARRFTLPQALAAVR
3D structure
PDB2y85 Bisubstrate Specificity in Histidine/Tryptophan Biosynthesis Isomerase from Mycobacterium Tuberculosis by Active Site Metamorphosis.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D11 D130
Catalytic site (residue number reindexed from 1) D10 D122
Enzyme Commision number 5.3.1.16: 1-(5-phosphoribosyl)-5- [(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase.
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 B D11 H50 V52 L54 S81 R143 D175 G176 S200 G201 V225 G226 K227 D10 H42 V44 L46 S73 R135 D167 G168 S192 G193 V217 G218 K219
Gene Ontology
Molecular Function
GO:0003949 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity
GO:0004640 phosphoribosylanthranilate isomerase activity
GO:0016853 isomerase activity
Biological Process
GO:0000105 L-histidine biosynthetic process
GO:0000162 tryptophan biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2y85, PDBe:2y85, PDBj:2y85
PDBsum2y85
PubMed21321225
UniProtP9WMM5|HIS4_MYCTU Phosphoribosyl isomerase A (Gene Name=priA)

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