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Structure of the capsid protein P1 of the bacteriophage PHI8

Analyse Structure of the capsid protein P1 of the bacteriophage PHI8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BTP
Type: protein
Length: 7,490 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P1
UniProt: Q9MC13
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	P1	protein	749	43% helix, 16% strand	Q9MC13

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	808	0.85	0.87	83	empty
2	1006	0.84	0.85	99	empty
3	963	0.84	0.85	83	empty
4	993	0.83	0.84	84	empty
5	982	0.83	0.84	82	empty

Interfaces

15 interfaces between chains.

A–B · 1957 Å² buried · 29 hydrogen bonds · protein-protein
E–I · 1938 Å² buried · 26 hydrogen bonds · protein-protein
H–I · 1929 Å² buried · 28 hydrogen bonds · protein-protein
A–J · 1925 Å² buried · 28 hydrogen bonds · protein-protein
E–F · 1923 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

4BTP · Structure of the capsid protein P1 of the bacteriophage phi8 · 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 Q9MC13
Elsewhere: RCSB PDB 4BTP · PDBe 4BTP · UniProt Q9MC13

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