Structure of PDB 1uin Chain A

Receptor sequence

>1uinA (length=350) Species: 274 (Thermus thermophilus)

RPPLIERYRNLLPVSEKTPVISLLEGSTPLIPLKGPEEARKKGIRLYAKY
EGLNPTGSFKDRGMTLAVSKAVEGGAQAVACASTGNTAASAAAYAARAGI
LAIVVLPAGYVALGKVAQSLVHGARIVQVEGNFDDALRLTQKLTEAFPVA
LVNSVNPHRLEGQKTLAFEVVDELGDAPHYHALPVGNAGNITAHWMGYKA
YHALGKAKRLPRMLGFQAAGAAPLVLGRPVERPETLATAIRIGNPASWQG
AVRAKEESGGVIEAVTDEEILFAYRYLAREEGIFCEPASAAAMAGVFKLL
REGRLEPESTVVLTLTGHGLKDPATAERVAELPPPVPARLEAVAAAAGLL

3D structure

• PDB: 1uin Crystal Structures of Threonine Synthase from Thermus thermophilus HB8: Conformational change, substrate recognition, and mechanism.
• Chain: A
• Resolution: 2.25 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K61 T85 P212 G216 Q218 A240 T317
• Catalytic site (residue number reindexed from 1): K60 T84 P211 G215 Q217 A239 T316
• 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	F60 K61 N87 V186 G187 N188 A189 G190 N191 A240 E287 T317 G318	F59 K60 N86 V185 G186 N187 A188 G189 N190 A239 E286 T316 G317

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

External links

• PDB: RCSB:1uin, PDBe:1uin, PDBj:1uin
• PDBsum: 1uin
• PubMed: 12952961
• UniProt: P83823