Structure of PDB 3ng0 Chain A Binding Site BS02

Receptor Information
>3ng0 Chain A (length=465) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RTPQEVLKWIQDENIKIIDLKFIDTPGIWQHCSFYYDQLDENSFTEGIPF
DGSSIRGWKAINESDMCMVPDPNTATIDPFCKEPTLSMICSIKEPRTGEW
YNRDPRTIAAKAAEYLRGTGIADTVYFGPEAEFFLFDDIRFGQTENSSYY
FADSVEGRWNTGREEEGGNLGYKPGYKQGYFPVAPTDTAQDIRTEMLLTM
AAFGVPIEKHHHEVASGGQNELGIKFDKLVNSADNLMIYKYVIKNVAKKY
GKTVTFMPKPIFNDNGSGMHVHQSLWKDGQPLFAGDKYAGFSQMGLWYIG
GILKHAPALLAFTNPTTNSYKRLVPGFEAPVNLAYSQGNRSASVRIPLSG
GNPKAKRLEFRCPDATSNPYLAFAAMLCAGIDGIKNQIDPGEPLDVDIEL
AKIPSTPGSLEAALEALEKDHEFLTGTGVFSPDFVESWIEYKLDNEVNPM
RLRPHPYEFSLYYDC
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain3ng0 Chain A Residue 475 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3ng0 Crystal Structure of Glutamine Synthetase from Synechocystis sp. PCC 6803
Resolution2.8 Å
Binding residue
(original residue number in PDB)		E134 E215 E223
Binding residue
(residue number reindexed from 1)		E132 E213 E221
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D53 E132 E134 E215 E223 H272 R342 E361 R363
Catalytic site (residue number reindexed from 1) D51 E130 E132 E213 E221 H270 R340 E359 R361
Enzyme Commision number 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:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0019676 ammonia assimilation cycle
GO:0019740 nitrogen utilization
Cellular Component
GO:0005737 cytoplasm
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:3ng0, PDBe:3ng0, PDBj:3ng0
PDBsum3ng0
PubMed
UniProtP77961|GLN1B_SYNY3 Glutamine synthetase (Gene Name=glnA)

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