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FAD and NADH binding domain of methane monooxygenase reductase from methylococcus capsulatus (bath)

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

PDB: 1TVC
Type: protein
Length: 250 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methane monooxygenase component C
EC: 1.14.13.25
UniProt: P22868
Ligands: FDA
Pockets: 2 · best druggability 0.54

Structure

solution nmr · 1 distinct chain · 21% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methane monooxygenase component C (EC 1.14.13.25)	protein	250	21% helix, 25% strand	P22868

Ligands and binding sites

FDA · Dihydroflavine-adenine dinucleotide · 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	185	0.54	0.79	32	FDA
2	95	0.53	0.83	21	empty

Compared structures

1TVC · FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus… · the same entry in another collection · chain A against A, TM-score 1.00
P22868 · AlphaFold monomer V2.0 prediction for methane monooxygenase component C (P22868) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 P22868
Elsewhere: RCSB PDB 1TVC · PDBe 1TVC · UniProt P22868

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