Research workbench

Long-chain alkane monooxygenase (lada) in complex with coenzyme FMN

Analyse Long-chain alkane monooxygenase (lada) in complex with coenzyme FMN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3B9O
Type: protein
Length: 866 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alkane monoxygenase
EC: 1.14.15.-
UniProt: A4IU28
Ligands: FMN
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alkane monoxygenase (EC 1.14.15.-)	protein	433	44% helix, 17% strand	A4IU28

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

7 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	644	0.78	0.83	63	FMN
2	719	0.76	0.81	55	FMN
3	498	0.71	0.80	47	empty
4	53	0.31	0.77	20	empty
5	74	0.29	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 3429 Å² buried · 45 hydrogen bonds · protein-protein

Compared structures

3B9O · long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN · 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 A4IU28
Elsewhere: RCSB PDB 3B9O · PDBe 3B9O · UniProt A4IU28

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