Structure of PDB 2c2g Chain B

Receptor sequence
>2c2gB (length=437) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
EDNIRRSNAVNPFSAKYVPFNAAPGSTESYSLDEIVYRSRSGGLLDVEHD
MEALKRFDGAYWRDLFDSRVGKSTWPYGSGVWSKKEWVLPEIDDDDIVSA
FEGNSNLFWAERFGKQFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNR
LRKMKRPVVGVGCASTGDTSAALSAYCASAGIPSIVFLPANKISMAQLVQ
PIANGAFVLSIDTDFDGCMKLIREITAELPIYLANSLNSLRLEGQKTAAI
EILQQFDWQVPDWVIVPGGNLGNIYAFYKGFKMCQELGLVDRIPRMVCAQ
AANANPLYLHYKSGWKDFKPVSIDRAVYALKKCNGIVEEATEEELMDAMA
QADSTGMFICPHTGVALTALFKLRNQGVIAPTDRTVVVSTAHGLKFTQSK
IDYHSNAIPDMACRFSNPPVDVKADFGAVMDVLKSYL
3D structure
PDB2c2g Allosteric Threonine Synthase: Reorganization of the Pyridoxal Phosphate Site Upon Asymmetric Activation Through S-Adenosylmethionine Binding to a Novel Site.
ChainB
Resolution2.61 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.3.1: threonine synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PLP B K163 T195 S262 R267 N296 N299 K137 T169 S236 R241 N270 N273
Gene Ontology
Molecular Function
GO:0004795 threonine synthase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009088 threonine biosynthetic process
Cellular Component
GO:0005886 plasma membrane
GO:0009507 chloroplast
GO:0009570 chloroplast stroma

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2c2g, PDBe:2c2g, PDBj:2c2g
PDBsum2c2g
PubMed16319072
UniProtQ9S7B5|THRC1_ARATH Threonine synthase 1, chloroplastic (Gene Name=TS1)

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