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Asymmetric unit for the coat proteins of phage qbeta

Analyse Asymmetric unit for the coat proteins of phage qbeta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VLY
Type: protein
Length: 388 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: P03615
Pockets: 7 · best druggability 0.73

Structure

electron microscopy · 3 distinct chains · 11% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein	protein	129	11% helix, 26% strand	P03615
B	Capsid protein	protein	132	11% helix, 26% strand	P03615
C	Capsid protein	protein	127	11% helix, 27% strand	P03615

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	903	0.73	0.77	92	empty
2	218	0.52	0.77	35	empty
3	146	0.44	0.76	23	empty
4	53	0.36	0.79	13	empty
5	78	0.31	0.73	19	empty

Interfaces

3 interfaces between chains.

B–C · 514 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 460 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 459 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5VLY · Asymmetric unit for the coat proteins of phage Qbeta · 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 P03615
Elsewhere: RCSB PDB 5VLY · PDBe 5VLY · UniProt P03615

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