Structure of PDB 2whi Chain A

Receptor sequence
>2whiA (length=476) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
EKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLA
FDGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLE
PYSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSF
YEVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKM
LTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNT
AWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTA
RHYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVR
IPITGSNPKAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVD
KDLYELPPEEAASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETWI
SFKRENEIEPVNIRPHPYEFALYYDV
3D structure
PDB2whi Structural Basis for the Inhibition of Mycobacterium Tuberculosis Glutamine Synthetase by Novel ATP-Competitive Inhibitors.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D54 E133 E135 E219 E227 H276 R347 E366 R368
Catalytic site (residue number reindexed from 1) D52 E131 E133 E217 E225 H274 R345 E364 R366
Enzyme Commision number 6.3.1.2: glutamine synthetase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0001968 fibronectin binding
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0035375 zymogen binding
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0010756 positive regulation of plasminogen activation
GO:0019740 nitrogen utilization
GO:0051260 protein homooligomerization
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2whi, PDBe:2whi, PDBj:2whi
PDBsum2whi
PubMed19695264
UniProtP9WN39|GLN1B_MYCTU Glutamine synthetase (Gene Name=glnA1)

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