MolNFT v1 · #13973 · protein

Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized FE(III)

1LTV · Phenylalanine-4-hydroxylase: “Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized…”. X-ray diffraction, 1 ligand (FE), 2 pockets (best druggability 0.68). MolNFT v1 #13973 on…

PDB: 1LTV
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phenylalanine-4-hydroxylase
EC: 1.14.16.1
UniProt: P30967
Ligands: FE
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylalanine-4-hydroxylase (EC 1.14.16.1)	protein	275	47% helix, 12% strand	P30967

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

2 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	292	0.68	0.82	33	empty
2	50	0.35	0.79	17	empty

Compared structures

1LTV · CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE WITH… · the same entry in another collection · chain A against A, TM-score 1.00
P30967 · AlphaFold monomer V2.0 prediction for phenylalanine-4-hydroxylase (P30967) · 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 P30967
Elsewhere: RCSB PDB 1LTV · PDBe 1LTV · UniProt P30967

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