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P4 protein from bacteriophage PHI8

Analyse P4 protein from bacteriophage PHI8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BLQ
Type: protein
Length: 1,602 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P4
EC: 3.6.1.15
UniProt: Q9MC14
Pockets: 20 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	P4 (EC 3.6.1.15)	protein	267	33% helix, 30% strand	Q9MC14

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	654	0.70	0.78	66	empty
2	235	0.66	0.84	38	empty
3	218	0.66	0.84	38	empty
4	228	0.65	0.83	37	empty
5	212	0.65	0.83	39	empty

Interfaces

6 interfaces between chains.

B–C · 1054 Å² buried · 13 hydrogen bonds · protein-protein
B–D · 1053 Å² buried · 13 hydrogen bonds · protein-protein
D–E · 1050 Å² buried · 17 hydrogen bonds · protein-protein
A–F · 1047 Å² buried · 14 hydrogen bonds · protein-protein
E–F · 1045 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4BLQ · P4 protein from 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 Q9MC14
Elsewhere: RCSB PDB 4BLQ · PDBe 4BLQ · UniProt Q9MC14

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