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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: 5KIP
Type: protein
Length: 390 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Coat protein
UniProt: P03615
Pockets: 7 · best druggability 0.75

Structure

electron microscopy · 2 distinct chains · 10% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Coat protein	protein	129	10% helix, 32% strand	P03615
B	Coat protein	protein	132	10% helix, 33% strand	P03615

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1036	0.75	0.77	110	empty
2	164	0.41	0.72	25	empty
3	106	0.39	0.76	19	empty
4	88	0.39	0.77	15	empty
5	54	0.34	0.78	12	empty

Interfaces

3 interfaces between chains.

B–C · 588 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 509 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 505 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5KIP · 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 5KIP · PDBe 5KIP · UniProt P03615

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