Structure of PDB 4xyc Chain E

Receptor sequence

>4xycE (length=463) Species: 1773 (Mycobacterium tuberculosis)

KTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLAF
DSDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEPYSRDPRNIARKA
ENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSFYEVDAISGWWNTG
AATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKMLTNLINSGFILEK
GHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNTAWQNGKTVTFMPK
PLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTARHYIGGLLHHAPS
LLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRIPITGSNPKAKRL
EFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDKDLYELPPEEAAS
IPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETWISFKRENEIEPVNI
RPHPYEFALYYDV

3D structure

• PDB: 4xyc Nanomolar inhibitors of Mycobacterium tuberculosis glutamine synthetase 1: Synthesis, biological evaluation and X-ray crystallographic studies.
• Chain: E
• 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): D51 E118 E120 E204 E212 H261 R332 E351 R353
• 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	E	Y125 F228 H274 S276 W278 K357 A358 R360	Y114 F217 H263 S265 W267 K346 A347 R349

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)