Structure of PDB 1htq Chain A

Receptor sequence
>1htqA (length=477) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
TEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGL
AFDGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTL
EPYSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGS
FYEVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDK
MLTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKN
TAWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDT
ARHYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACV
RIPITGSNPKAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPV
DKDLYELPPEEAASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETW
ISFKRENEIEPVNIRPHPYEFALYYDV
3D structure
PDB1htq Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D50 E129 E131 E212 E220 H269 R339 E357 R359
Catalytic site (residue number reindexed from 1) D53 E132 E134 E218 E226 H275 R346 E365 R367
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 MN A E129 H269 E357 R359 E132 H275 E365 R367
BS02 AMP A Y125 G127 E129 F225 H271 S273 W275 R355 Y128 G130 E132 F231 H277 S279 W281 R363
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1htq, PDBe:1htq, PDBj:1htq
PDBsum1htq
PubMed12146952
UniProtP9WN39|GLN1B_MYCTU Glutamine synthetase (Gene Name=glnA1)

[Back to BioLiP]