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Structure of the mimivirus genomic fibre in its relaxed 5-start helix form

Analyse Structure of the mimivirus genomic fibre in its relaxed 5-start helix form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7YX5
Type: protein
Length: 645 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glucose-methanol-choline oxidoreductase protein
UniProt: E5L7Z5
Ligands: FAD
Pockets: 8 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 32% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative glucose-methanol-choline oxidoreductase protein	protein	645	32% helix, 17% strand	E5L7Z5

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

8 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	935	0.83	0.85	84	FAD
2	85	0.53	0.84	21	empty
3	71	0.48	0.83	16	empty
4	63	0.43	0.82	16	empty
5	55	0.37	0.80	20	empty

Compared structures

7YX5 · Structure of the Mimivirus genomic fibre in its relaxed 5-start helix form · 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 E5L7Z5
Elsewhere: RCSB PDB 7YX5 · PDBe 7YX5 · UniProt E5L7Z5

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