Structure of PDB 2qc8 Chain A Binding Site BS05

Receptor Information

>2qc8 Chain A (length=356) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

NKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPE
WNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPA
ETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQG
PYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPC
EGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTK
AMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNI
NDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTC
LLNETG

Ligand information

Ligand ID

P3S

InChI

InChI=1S/C5H13N2O6PS/c1-15(13,7-14(10,11)12)3-2-4(6)5(8)9/h4H,2-3,6H2,1H3,(H,8,9)(H2,10,11,12)/t4-,15-/m0/s1

InChIKey

QQFOFBSCSWFFPB-NMAPHRJESA-N

SMILES

Software	SMILES
ACDLabs 10.04	O=P(N=S(=O)(CCC(N)C(=O)O)C)(O)O
CACTVS 3.341	C[S](=O)(CC[C@H](N)C(O)=O)=N[P](O)(O)=O
CACTVS 3.341	C[S](=O)(CC[CH](N)C(O)=O)=N[P](O)(O)=O
OpenEye OEToolkits 1.5.0	CS(=NP(=O)(O)O)(=O)CCC(C(=O)O)N
OpenEye OEToolkits 1.5.0	C[S@](=NP(=O)(O)O)(=O)CC[C@@H](C(=O)O)N

Formula

C5 H13 N2 O6 P S

Name

L-METHIONINE-S-SULFOXIMINE PHOSPHATE

PDB chain

2qc8 Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2qc8 Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
Resolution	2.6 Å
Binding residue (original residue number in PDB)	E134 E136 E196 E203 G249 H253 R299 E305 R319 R340
Binding residue (residue number reindexed from 1)	E125 E127 E187 E194 G240 H244 R290 E296 R310 R331
Annotation score	2

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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Cellular Component

External links

PDB	RCSB:2qc8, PDBe:2qc8, PDBj:2qc8
PDBsum	2qc8
PubMed	18005987
UniProt	P15104\|GLNA_HUMAN Glutamine synthetase (Gene Name=GLUL)

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