Structure of PDB 2zsj Chain D

Receptor sequence
>2zsjD (length=348) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
RWQGIIKQYKKYLPVDENTPIVTLYEGNTPLIEADNLARAIGFKGKIYLK
YEGLNPTGSFKDRGMTLAISKAVEAGKRAVICASTGNTSASAAAYAARAG
LRAYVLLPKGAIGKLSQAMIYGAKVLAIQGTFDDALNIVRKIGENFPVEI
VNSVNPYRIEGQKTAAFEICDTLGEAPDYHFIPVGNAGNITAYWKGFKIY
YEEGKITKLPRMMGWQAEGAAPIVKGYPIKNPQTIATAIKIGNPYSWKSA
LKAAQESGGKIDAVSDSEILYAYKLIASTEGVFCEPASAASVAGLIKLVR
EGFFKGGEVVTCTLTGNGLKDPDTAIKVCEEPITVPPDFDEVVKVLGF
3D structure
PDB2zsj Crystal structure of threonine synthase from Aquifex aeolicus VF5
ChainD
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K63 T87 Q220 A224 A242 T319
Catalytic site (residue number reindexed from 1) K61 T85 Q216 A220 A238 T315
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 D F62 K63 N89 V188 G189 N190 A191 G192 N193 A242 E289 T319 G320 F60 K61 N87 V184 G185 N186 A187 G188 N189 A238 E285 T315 G316
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
GO:0019344 cysteine biosynthetic process
GO:1901605 alpha-amino acid metabolic 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:2zsj, PDBe:2zsj, PDBj:2zsj
PDBsum2zsj
PubMed
UniProtO66740

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