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The structure of thcox, the first oxidase protein from the cyanobactin pathways

Analyse The structure of thcox, the first oxidase protein from the cyanobactin pathways in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LQ4
Type: protein
Length: 922 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyagox
UniProt: B8HTZ1
Ligands: FMN
Pockets: 14 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyagox	protein	457	35% helix, 23% strand	B8HTZ1
B	Cyagox	protein	465	35% helix, 23% strand	B8HTZ1

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

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

Pockets

14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	933	0.77	0.80	98	FMN
2	496	0.62	0.75	53	empty
3	371	0.61	0.77	47	FMN
4	60	0.47	0.84	17	empty
5	97	0.44	0.79	20	empty

Interfaces

1 interface between chains.

A–B · 4516 Å² buried · 51 hydrogen bonds · protein-protein

Compared structures

5LQ4 · The Structure of ThcOx, the First Oxidase Protein from the Cyanobactin Pathways · 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 B8HTZ1
Elsewhere: RCSB PDB 5LQ4 · PDBe 5LQ4 · UniProt B8HTZ1

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