Research workbench

Human homogentisate dioxygenase with FE(II)

Analyse Human homogentisate dioxygenase with FE(II) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EY2
Type: protein
Length: 419 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Homogentisate 1,2-dioxygenase
EC: 1.13.11.5
UniProt: Q93099
Ligands: FE2
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Homogentisate 1,2-dioxygenase (EC 1.13.11.5)	protein	419	8% helix, 39% strand	Q93099

Ligands and binding sites

FE2 · Fe (II) ion · metal · chains A

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	482	0.67	0.78	49	empty
2	134	0.50	0.80	27	empty
3	121	0.38	0.74	20	empty
4	52	0.34	0.79	17	empty
5	65	0.30	0.75	20	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

1EY2 · Human homogentisate dioxygenase with FE(II) · the same entry in another collection · chain A against A, TM-score 1.00
Q93099 · AlphaFold monomer V2.0 prediction for homogentisate 1,2-dioxygenase (Q93099) · 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 Q93099
Elsewhere: RCSB PDB 1EY2 · PDBe 1EY2 · UniProt Q93099

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