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Crystal structure of the apo form of a quaternary ammonium rieske monooxygenase cnta

Analyse Crystal structure of the apo form of a quaternary ammonium rieske monooxygenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Y8J
Type: protein
Length: 343 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carnitine monooxygenase oxygenase subunit
EC: 1.14.13.239
UniProt: A0A059ZPP5
Ligands: FES
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carnitine monooxygenase oxygenase subunit (EC 1.14.13.239)	protein	343	26% helix, 30% strand	A0A059ZPP5

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	321	0.69	0.82	31	empty
2	185	0.56	0.79	22	empty

Compared structures

6Y8J · Crystal structure of the apo form of a quaternary ammonium Rieske monooxygenase CntA · 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 A0A059ZPP5
Elsewhere: RCSB PDB 6Y8J · PDBe 6Y8J · UniProt A0A059ZPP5

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