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Bacteriophage P22 mature virion capsid protein

Analyse Bacteriophage P22 mature virion capsid protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UU5
Type: protein
Length: 3,010 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major capsid protein
UniProt: P26747
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 19% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
G, A, C, E, F, B, D	Major capsid protein	protein	430	19% helix, 31% strand	P26747

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	190	0.83	0.97	33	empty
2	178	0.83	0.97	32	empty
3	159	0.81	0.97	24	empty
4	121	0.81	0.98	22	empty
5	128	0.79	0.97	23	empty

Interfaces

14 interfaces between chains.

E–F · 3446 Å² buried · 48 hydrogen bonds · protein-protein
C–B · 3427 Å² buried · 45 hydrogen bonds · protein-protein
A–B · 3414 Å² buried · 56 hydrogen bonds · protein-protein
C–D · 3355 Å² buried · 54 hydrogen bonds · protein-protein
A–F · 3329 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

5UU5 · Bacteriophage P22 mature virion 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
Every structure of UniProt P26747
Elsewhere: RCSB PDB 5UU5 · PDBe 5UU5 · UniProt P26747

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