Research workbench

Crystal structure of di-iron aurf

Analyse Crystal structure of di-iron aurf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CHU
Type: protein
Length: 597 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P-aminobenzoate N-oxygenase
UniProt: Q70KH9
Ligands: FEO
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P-aminobenzoate N-oxygenase	protein	294	69% helix, 1% strand	Q70KH9
B	P-aminobenzoate N-oxygenase	protein	303	67% helix, 1% strand	Q70KH9

Ligands and binding sites

FEO · Mu-oxo-diiron · ligand · 2 copies · chains A, B

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	527	0.78	0.85	62	empty
2	670	0.78	0.83	89	empty
3	76	0.37	0.77	15	empty
4	67	0.29	0.74	14	empty
5	59	0.29	0.74	12	empty

Interfaces

1 interface between chains.

A–B · 1189 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3CHU · Crystal Structure of Di-iron Aurf · the same entry in another collection · chain A against A, TM-score 1.00

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 Q70KH9
Elsewhere: RCSB PDB 3CHU · PDBe 3CHU · UniProt Q70KH9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.