Structure of PDB 3it6 Chain A Binding Site BS01

Receptor Information
>3it6 Chain A (length=193) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTRLLRAQGVTAPAGFRAAGVAAGIKASGALDLALVFNEGPDYAAAGVFT
RNQVKAAPVLWTQQVLTTGRLRAVILNSGGANACTGPAGFADTHATAEAV
AAALSDWGTETGAIEVAVCSTGLIGDRLPMDKLLAGVAHVVHEMHGGLVG
GDEAAHAIMTTDNVPKQVALHHHDNWTVGGMAKGAGMLAPSLA
Ligand information
Ligand IDORN
InChIInChI=1S/C5H12N2O2/c6-3-1-2-4(7)5(8)9/h4H,1-3,6-7H2,(H,8,9)/t4-/m0/s1
InChIKeyAHLPHDHHMVZTML-BYPYZUCNSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(C[C@@H](C(=O)O)N)CN
CACTVS 3.370NCCC[CH](N)C(O)=O
CACTVS 3.370NCCC[C@H](N)C(O)=O
ACDLabs 12.01O=C(O)C(N)CCCN
OpenEye OEToolkits 1.7.6C(CC(C(=O)O)N)CN
FormulaC5 H12 N2 O2
NameL-ornithine
ChEMBLCHEMBL446143
DrugBankDB00129
ZINCZINC000001532530
PDB chain3it6 Chain B Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3it6 The molecular structure of ornithine acetyltransferase from Mycobacterium tuberculosis bound to ornithine, a competitive inhibitor.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		T166 M193
Binding residue
(residue number reindexed from 1)		T160 M187
Annotation score5
Enzymatic activity
Enzyme Commision number 2.3.1.1: amino-acid N-acetyltransferase.
2.3.1.35: glutamate N-acetyltransferase.
Gene Ontology
Molecular Function
GO:0004358 glutamate N-acetyltransferase activity
Biological Process
GO:0006526 L-arginine biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3it6, PDBe:3it6, PDBj:3it6
PDBsum3it6
PubMed20184895
UniProtP9WPZ3|ARGJ_MYCTU Arginine biosynthesis bifunctional protein ArgJ (Gene Name=argJ)

[Back to BioLiP]