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Structure of F420-H2 dependent oxidoreductase (fdor-a) MSMEG_2027 in complex with F420

Analyse Structure of F420-H2 dependent oxidoreductase (fdor-a) MSMEG_2027 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WTA
Type: protein
Length: 143 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: A0QU01
Ligands: UBM
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	137	30% helix, 34% strand	A0QU01
Z	Uncharacterized protein	protein	6	0% helix, 0% strand	A0QU01

Ligands and binding sites

UBM · Coenzyme F420-4 · ligand · chains A, Z

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	253	0.65	0.82	28	UBM

Interfaces

1 interface between chains.

A–Z · 356 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6WTA · Structure of F420-H2 Dependent Oxidoreductase (FDOR-A) MSMEG_2027 in complex with F420 · 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 A0QU01
Elsewhere: RCSB PDB 6WTA · PDBe 6WTA · UniProt A0QU01

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