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Major capsid protein P1 of the pseudomonas phage PHI6

Analyse Major capsid protein P1 of the pseudomonas phage PHI6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4K7H
Type: protein
Length: 3,800 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major inner protein P1
UniProt: P11126
Pockets: 20 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Major inner protein P1	protein	760	48% helix, 12% strand	P11126

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	1064	0.88	0.90	123	empty
2	1110	0.88	0.89	119	empty
3	865	0.86	0.89	91	empty
4	944	0.84	0.86	90	empty
5	597	0.84	0.89	78	empty

Interfaces

5 interfaces between chains.

D–E · 1793 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1763 Å² buried · 19 hydrogen bonds · protein-protein
B–E · 1747 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 1744 Å² buried · 15 hydrogen bonds · protein-protein
C–D · 1726 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4K7H · Major capsid protein P1 of the Pseudomonas phage phi6 · 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 P11126
Elsewhere: RCSB PDB 4K7H · PDBe 4K7H · UniProt P11126

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