Structure of PDB 1htq Chain U Binding Site BS02
Receptor Information
>1htq Chain U (length=477) Species:
1773
(Mycobacterium tuberculosis) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
TEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGL
AFDGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTL
EPYSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGS
FYEVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDK
MLTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKN
TAWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDT
ARHYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACV
RIPITGSNPKAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPV
DKDLYELPPEEAASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETW
ISFKRENEIEPVNIRPHPYEFALYYDV
Ligand information
Ligand ID
AMP
InChI
InChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKey
UDMBCSSLTHHNCD-KQYNXXCUSA-N
SMILES
Software
SMILES
CACTVS 3.370
Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370
Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6
c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
ACDLabs 12.01
O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
Formula
C10 H14 N5 O7 P
Name
ADENOSINE MONOPHOSPHATE
ChEMBL
CHEMBL752
DrugBank
DB00131
ZINC
ZINC000003860156
PDB chain
1htq Chain U Residue 7515 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure 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
]
PDB
1htq
Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation.
Resolution
2.4 Å
Binding residue
(original residue number in PDB)
Y125 G127 E129 F225 H271 S273 W275 R355
Binding residue
(residue number reindexed from 1)
Y128 G130 E132 F231 H277 S279 W281 R363
Annotation score
4
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.
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
PDBsum
1htq
PubMed
12146952
UniProt
P9WN39
|GLN1B_MYCTU Glutamine synthetase (Gene Name=glnA1)
[
Back to BioLiP
]