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MolNFT v1 · #50949 · protein

Tyrosine hydroxylase catalytic and tetramerization domains from rat

2TOH · Tyrosine 3-monooxygenase: “Tyrosine hydroxylase catalytic and tetramerization domains from rat”. X-ray diffraction, 3 ligands (HBI, FE, CL), 1 pocket (best druggability 0.76). MolNFT v1 #50949 on GenesisL1: 3D structure, binding…

PDB
2TOH
Type
protein
Length
336 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine 3-monooxygenase
EC
1.14.16.2
UniProt
P04177
Ligands
HBI, FE, CL
Pockets
1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine 3-monooxygenase (EC 1.14.16.2)protein33651% helix, 12% strandP04177

Ligands and binding sites

  • HBI · 7,8-dihydrobiopterin · ligand · chains A
  • FE · Fe (III) ion · metal · chains A
  • CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15780.760.8358HBI

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 2TOH · Tyrosine hydroxylase catalytic and tetramerization domains from rat · the same entry in another collection · chain A against A, TM-score 1.00
  • P04177 · AlphaFold monomer V2.0 prediction for tyrosine 3-monooxygenase (P04177) · a predicted model of the same protein · chain A against A, TM-score 0.99

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