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Crystal structure of C. violaceum phenylalanine hydroxylase D139A mutation

Analyse Crystal structure of C. violaceum phenylalanine hydroxylase D139A mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Q3Y
Type: protein
Length: 269 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: CO
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylalanine-4-hydroxylase (EC 1.14.16.1)	protein	269	48% helix, 10% strand	P30967

Ligands and binding sites

CO · Cobalt (II) 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	386	0.63	0.78	40	empty
2	58	0.39	0.80	14	empty

Compared structures

4Q3Y · Crystal structure of C. violaceum phenylalanine hydroxylase D139A mutation · 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 4Q3Y · PDBe 4Q3Y · UniProt P30967

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