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Soluble methane monooxygenase reductase FAD-binding domain from methylosinus sporium.

Analyse Soluble methane monooxygenase reductase FAD-binding domain from methylosinus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6L2U
Type: protein
Length: 206 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methane monooxygenase
UniProt: Q27RN2
Ligands: FAD
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Methane monooxygenase	protein	103	13% helix, 44% strand	Q27RN2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	532	0.76	0.83	43	FAD

Interfaces

1 interface between chains.

A–B · 606 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6L2U · Soluble methane monooxygenase reductase FAD-binding domain from Methylosinus sporium. · 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 Q27RN2
Elsewhere: RCSB PDB 6L2U · PDBe 6L2U · UniProt Q27RN2

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