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Flip major capsid protein

Analyse Flip major capsid protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OAC
Type: protein
Length: 3,100 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major capsid protein
Pockets: 20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 13% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	Major capsid protein	protein	310	13% helix, 28% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	942	0.88	0.90	132	empty
2	853	0.80	0.83	101	empty
3	369	0.77	0.88	52	empty
4	932	0.76	0.79	88	empty
5	602	0.76	0.82	89	empty

Interfaces

18 interfaces between chains.

D–E · 1514 Å² buried · 21 hydrogen bonds · protein-protein
A–C · 1508 Å² buried · 19 hydrogen bonds · protein-protein
H–I · 1506 Å² buried · 17 hydrogen bonds · protein-protein
G–H · 1482 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 1474 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

5OAC · FLiP major capsid protein · the same entry in another collection · chain G against G, 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
Elsewhere: RCSB PDB 5OAC · PDBe 5OAC

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