Structure of PDB 3aex Chain B Binding Site BS02

Receptor Information

>3aex Chain B (length=351) Species: 300852 (Thermus thermophilus HB8)

MRPPLIERYRNLLPVSEKTPVISLLEGSTPLIPLKGPEEARKKGIRLYAK
YEGLNPTGSFKDRGMTLAVSKAVEGGAQAVACASTGNTAASAAAYAARAG
ILAIVVLPAGYVALGKVAQSLVHGARIVQVEGNFDDALRLTQKLTEAFPV
ALVNSVNPHRLEGQKTLAFEVVDELGDAPHYHALPVGNAGNITAHWMGYK
AYHALGKAKRLPRMLGFQAAGAAPLVLGRPVERPETLATAIRIGNPASWQ
GAVRAKEESGGVIEAVTDEEILFAYRYLAREEGIFCEPASAAAMAGVFKL
LREGRLEPESTVVLTLTGHGLKDPATAERVAELPPPVPARLEAVAAAAGL
L

Ligand information

• Ligand ID: PO4
• InChI: InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
• InChIKey: NBIIXXVUZAFLBC-UHFFFAOYSA-K
• SMILES:
  CACTVS 3.341: [O-][P]([O-])([O-])=O
  ACDLabs 10.04: [O-]P([O-])([O-])=O
  OpenEye OEToolkits 1.5.0: [O-]P(=O)([O-])[O-]
• Formula: O4 P
• Name: PHOSPHATE ION
• DrugBank: DB14523
• PDB chain: 3aex Chain B Residue 6267

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3aex Product-assisted catalysis as the basis of the reaction specificity of threonine synthase.
• Resolution: 2.1 Å
• Binding residue (original residue number in PDB): K61 T88 F134 N154 S155 R160 N188
• Binding residue (residue number reindexed from 1): K61 T88 F134 N154 S155 R160 N188
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): K61 T85 P212 G216 Q218 A240 T317
• Catalytic site (residue number reindexed from 1): K61 T85 P212 G216 Q218 A240 T317
• Enzyme Commision number: 4.2.3.1: threonine synthase.

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:3aex, PDBe:3aex, PDBj:3aex
• PDBsum: 3aex
• PubMed: 21084312
• UniProt: Q5SL02