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Asfv core shell protein P15

Analyse Asfv core shell protein P15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LNL
Type: protein
Length: 448 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 60 kda polyprotein
UniProt: A0A0A1DY09
Pockets: 4 · best druggability 0.41

Structure

x-ray diffraction · 3 distinct chains · 28% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	60 kda polyprotein	protein	151	27% helix, 23% strand	A0A0A1DY09
B	60 kda polyprotein	protein	148	27% helix, 24% strand	A0A0A1DY09
C	60 kda polyprotein	protein	149	30% helix, 25% strand	A0A0A1DY09

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.41	0.79	16	empty
2	82	0.40	0.78	17	empty
3	51	0.33	0.77	15	empty
4	81	0.29	0.72	19	empty

Interfaces

3 interfaces between chains.

A–C · 458 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 435 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 431 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6LNL · ASFV core shell protein p15 · 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 A0A0A1DY09
Elsewhere: RCSB PDB 6LNL · PDBe 6LNL · UniProt A0A0A1DY09

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