MolNFT v2 · #215824 · protein

Knockout of GMC-oxidoreductase genes reveals that functional redundancy preserves mimivirus essential functions

8ORH · Putative GMC-type oxidoreductase: “Knockout of GMC-oxidoreductase genes reveals that functional redundancy preserves mimivirus essential…”. Electron microscopy at 4.2, 1 ligand (FAD), 20 pockets (best druggability 0.87). MolNFT v2…

PDB: 8ORH
Type: protein
Length: 1,298 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 4.2
Source: Mimivirus reunion
Molecule: Putative GMC-type oxidoreductase
UniProt: A0A8A5IZP6
Ligands: FAD
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · resolution 4.2 · 1 distinct chain · 31% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative GMC-type oxidoreductase	protein	649	31% helix, 19% strand	A0A8A5IZP6

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

20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1016	0.87	0.87	112	FAD
2	584	0.84	0.89	71	FAD
3	189	0.55	0.79	37	empty
4	125	0.52	0.81	22	empty
5	167	0.51	0.78	32	empty

Interfaces

1 interface between chains.

A–B · 2439 Å² buried · 30 hydrogen bonds · protein-protein

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 A0A8A5IZP6
Elsewhere: RCSB PDB 8ORH · PDBe 8ORH · UniProt A0A8A5IZP6

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