Structure of PDB 2ojw Chain A Binding Site BS04

Receptor Information
>2ojw Chain A (length=360) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YFQSMASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDS
EPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLC
EVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGDGHPFGWP
SNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPA
QWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGA
GCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEAL
IRTCLLNETG
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain2ojw Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2ojw Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
Resolution2.05 Å
Binding residue
(original residue number in PDB)		E134 E203 H253 R319
Binding residue
(residue number reindexed from 1)		E135 E203 H253 R314
Annotation score1
Enzymatic activity
Enzyme Commision number 2.3.1.225: protein S-acyltransferase.
6.3.1.2: glutamine synthetase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0016874 ligase activity
GO:0019706 protein-cysteine S-palmitoyltransferase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0001525 angiogenesis
GO:0006538 glutamate catabolic process
GO:0006542 glutamine biosynthetic process
GO:0008283 cell population proliferation
GO:0009267 cellular response to starvation
GO:0009749 response to glucose
GO:0010594 regulation of endothelial cell migration
GO:0018345 protein palmitoylation
GO:0042254 ribosome biogenesis
GO:1903670 regulation of sprouting angiogenesis
GO:1904749 regulation of protein localization to nucleolus
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0044297 cell body
GO:0070062 extracellular exosome
GO:0097386 glial cell projection

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2ojw, PDBe:2ojw, PDBj:2ojw
PDBsum2ojw
PubMed18005987
UniProtP15104|GLNA_HUMAN Glutamine synthetase (Gene Name=GLUL)

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