Structure of PDB 2d3a Chain E Binding Site BS02

Receptor Information
>2d3a Chain E (length=353) Species: 4577 (Zea mays) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CLTDLVNLNLSDTTEKIIAEYIWIGGSGMDLRSKARTLPGPVTDPSKLPK
WNYDGSSTGQAPGEDSEVILYPQAIFKDPFRRGNNILVMCDCYTPAGEPI
PTNKRYSAAKIFSSPEVAAEEPWYGIEQEYTLLQKDTNWPLGWPIGGFPG
PQGPYYCGIGAEKSFGRDIVDAHYKACLYAGINISGINGEVMPGQWEFQV
GPSVGISSGDQVWVARYILERITEIAGVVVTFDPKPIPGDWNGAGAHTNY
STESMRKEGGYEVIKAAIEKLKLRHKEHIAAYGEGNERRLTGRHETADIN
TFSWGVANRGASVRVGRETEQNGKGYFEDRRPASNMDPYVVTSMIAETTI
VWK
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 chain2d3a Chain E Residue 1042 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2d3a Atomic Structure of Plant Glutamine Synthetase: A KEY ENZYME FOR PLANT PRODUCTIVITY
Resolution2.63 Å
Binding residue
(original residue number in PDB)		E129 H249 E330
Binding residue
(residue number reindexed from 1)		E127 H247 E328
Annotation score1
Enzymatic activity
Enzyme Commision number 6.3.1.2: glutamine synthetase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006542 glutamine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2d3a, PDBe:2d3a, PDBj:2d3a
PDBsum2d3a
PubMed16829528
UniProtP38561|GLNA3_MAIZE Glutamine synthetase root isozyme 3 (Gene Name=GLN4)

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