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Tyrosine hydroxylase catalytic and tetramerization domains from rat

Analyse Tyrosine hydroxylase catalytic and tetramerization domains from rat in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TOH
Type: protein
Length: 325 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine hydroxylase
EC: 1.14.16.2
UniProt: P04177
Ligands: FE
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine hydroxylase (EC 1.14.16.2)	protein	325	52% helix, 12% strand	P04177

Ligands and binding sites

FE · Fe (III) ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	385	0.73	0.84	38	FE
2	62	0.33	0.76	16	empty
3	51	0.31	0.77	11	empty
4	51	0.29	0.75	13	empty

Compared structures

1TOH · 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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P04177
Elsewhere: RCSB PDB 1TOH · PDBe 1TOH · UniProt P04177

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