Structure of PDB 5cwa Chain A

Receptor sequence
>5cwaA (length=505) Species: 83331 (Mycobacterium tuberculosis CDC1551) [Search protein sequence]
ADLAATTSREDFRLLAAEHRVVPVTRKVLADSETPLSAYRKLAANRPGTF
LLESAENGRSWSRWSFIGAGAPTALTVREGQAVWLGAVPKDAPTGGDPLR
ALQVTLELLATADPGLPPLSGGMVGFFAYDMVRRLERLPERAVDDLCLPD
MLLLLATDVAAVDHHEGTITLIANAVNWNGTDERVDWAYDDAVARLDVMT
AALGQPLPSTVATFSRPEPRHRAQRTVEEYGAIVEYLVDQIAAGEAFQVV
PSQRFEMDTDVDPIDVYRILRVTNPSPYMYLLQVPNSDGAVDFSIVGSSP
EALVTVHEGWATTHPIAGTRWRGRTDDEDVLLEKELLADDKERAEHLMLV
DLGRNDLGRVCTPGTVRVEDYSHIERYSHVMHLVSTVTGKLGEGRTALDA
VTACFPAGTLSGAPKVRAMELIEEVEKTRRGLYGGVVGYLDFAGNADFAI
AIRTALMRNGTAYVQAGGGVVADSNGSYEYNEARNKARAVLNAIAAAETL
AAPGA
3D structure
PDB5cwa Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q254 E307 A323 E351 H388 T415 Y439 R459 G475 E488 K492
Catalytic site (residue number reindexed from 1) Q248 E301 A317 E345 H382 T409 Y433 R453 G469 E482 K486
Enzyme Commision number 4.1.3.27: anthranilate synthase.
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 0GA A Y439 I458 A472 G473 K492 Y433 I452 A466 G467 K486 MOAD: ic50=17uM
PDBbind-CN: -logKd/Ki=4.77,IC50=17uM
Gene Ontology
Molecular Function
GO:0004049 anthranilate synthase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5cwa, PDBe:5cwa, PDBj:5cwa
PDBsum5cwa
PubMed26527146
UniProtP9WFX2|TRPE_MYCTO Anthranilate synthase component 1 (Gene Name=trpE)

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