Structure of PDB 4xyc Chain D

Receptor sequence

>4xycD (length=466) Species: 1773 (Mycobacterium tuberculosis)

TEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGL
AFDGSDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEPYSRDPRNIA
RKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSFYEVDAISGWW
NTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKMLTNLINSGFI
LEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNTAWQNGKTVTF
MPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTARHYIGGLLHH
APSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRIPITGSNPKA
KRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDKDLYELPPEE
AASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETWISFKRENEIEP
VNIRPHPYEFALYYDV

3D structure

• PDB: 4xyc Nanomolar inhibitors of Mycobacterium tuberculosis glutamine synthetase 1: Synthesis, biological evaluation and X-ray crystallographic studies.
• Chain: D
• Resolution: 3.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D50 E129 E131 E215 E223 H272 R343 E362 R364
• Catalytic site (residue number reindexed from 1): D53 E121 E123 E207 E215 H264 R335 E354 R356
• Enzyme Commision number: 6.3.1.2: glutamine synthetase.

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	2K9	D	Y125 G127 F228 H274 S276 W278 K357 A358 R360	Y117 G119 F220 H266 S268 W270 K349 A350 R352

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004356 glutamine synthetase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006542 glutamine biosynthetic process
• GO:0019740 nitrogen utilization

Cellular Component

• GO:0005737 cytoplasm
• GO:0016020 membrane

External links

• PDB: RCSB:4xyc, PDBe:4xyc, PDBj:4xyc
• PDBsum: 4xyc
• PubMed: 25770781
• UniProt: P9WN38|GLN1B_MYCTO Glutamine synthetase (Gene Name=glnA1)