Structure of PDB 2c2g Chain A

Receptor sequence
>2c2gA (length=448) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
ETAVKPPHRTERRNRSNAVNPFSAKYVPFNAAPGSTESYSLDEIVYRSRS
GGLLDVEHDMEALKRFDGAYWRDLFDSRVGKSTWPYGSGVWSKKEWVLPE
IDDDDIVSAFEGNSNLFWAERFGKQFLGMNDLWVKHCGISHTGSFKDLGM
TVLVSQVNRLRKMKRPVVGVGCASTGDTSAALSAYCASAGIPSIVFLPAN
KISMAQLVQPIANGAFVLSIDTDFDGCMKLIREITAELPIYLANSLNSLR
LEGQKTAAIEILQQFDWQVPDWVIVPGGNLGNIYAFYKGFKMCQELGLVD
RIPRMVCAQAANANPLYLHYKSGWKDFKPVSIDRAVYALKKCNGIVEEAT
EEELMDAMAQADSTGMFICPHTGVALTALFKLRNQGVIAPTDRTVVVSTA
HGLKFTQSKIDYHSNAIPDMACRFSNPPVDVKADFGAVMDVLKSYLGS
3D structure
PDB2c2g Allosteric Threonine Synthase: Reorganization of the Pyridoxal Phosphate Site Upon Asymmetric Activation Through S-Adenosylmethionine Binding to a Novel Site.
ChainA
Resolution2.61 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A K163 S191 T195 S262 R267 N296 K146 S174 T178 S245 R250 N279
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

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

[Back to BioLiP]