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De novo model of bacteriophage P22 procapsid coat protein

Analyse De novo model of bacteriophage P22 procapsid coat protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XYY
Type: protein
Length: 2,912 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Coat protein
UniProt: A8CGC7
Pockets: 6 · best druggability 0.35

Structure

electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	Coat protein	protein	416	0% helix, 0% strand	A8CGC7

Pockets

6 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	95	0.35	0.72	26	empty
2	92	0.35	0.72	28	empty
3	77	0.33	0.73	23	empty
4	75	0.33	0.73	22	empty
5	53	0.30	0.74	16	empty

Interfaces

8 interfaces between chains.

A–G · 213 Å² buried · 0 hydrogen bonds · protein-protein
E–F · 164 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 115 Å² buried · 0 hydrogen bonds · protein-protein
A–F · 108 Å² buried · 0 hydrogen bonds · protein-protein
C–D · 106 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2XYY · De Novo model of Bacteriophage P22 procapsid coat protein · 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 A8CGC7
Elsewhere: RCSB PDB 2XYY · PDBe 2XYY · UniProt A8CGC7

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