Structure of PDB 2c2b Chain F

Receptor sequence
>2c2bF (length=444) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
VNPFSAKYVPFNAAPGSTESYSLDEIVYRSRSGGLLDVEHDMEALKRFDG
AYWRDLFDSRVGKSTWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFW
AERFGKQFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMKRPVV
GVGCASTGDTSAALSAYCASAGIPSIVFLPANKISMAQLVQPIANGAFVL
SIDTDFDGCMKLIREITAELPIYLANSLNSLRLEGQKTAAIEILQQFDWQ
VPDWVIVPGGNLGNIYAFYKGFKMCQELGLVDRIPRMVCAQAANANPLYL
HYKSGWKDFKPMTASTTFASAIQIGDPVSIDRAVYALKKCNGIVEEATEE
ELMDAMAQADSTGMFICPHTGVALTALFKLRNQGVIAPTDRTVVVSTAHG
LKFTQSKIDYHSNAIPDMACRFSNPPVDVKADFGAVMDVLKSYL
3D structure
PDB2c2b Allosteric Threonine Synthase: Reorganization of the Pyridoxal Phosphate Site Upon Asymmetric Activation Through S-Adenosylmethionine Binding to a Novel Site.
ChainF
Resolution2.6 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 SAM F N132 L133 W150 Q281 F282 N97 L98 W115 Q246 F247
BS02 SAM F S99 T100 W101 P102 G104 S105 F127 S64 T65 W66 P67 G69 S70 F92
BS03 PLP F F162 K163 D194 G294 G295 N296 L297 G298 N299 A356 H404 T432 F127 K128 D159 G259 G260 N261 L262 G263 N264 A321 H369 T397
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:2c2b, PDBe:2c2b, PDBj:2c2b
PDBsum2c2b
PubMed16319072
UniProtQ9S7B5|THRC1_ARATH Threonine synthase 1, chloroplastic (Gene Name=TS1)

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