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Crystal structure of MS2 capsids with mutations in the subunit fg loop

Analyse Crystal structure of MS2 capsids with mutations in the subunit fg loop in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MST
Type: protein
Length: 387 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bacteriophage MS2 capsid
UniProt: P03612
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Bacteriophage MS2 capsid	protein	129	19% helix, 47% strand	P03612

Pockets

4 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	979	0.76	0.78	112	empty
2	118	0.38	0.74	26	empty
3	96	0.34	0.74	17	empty
4	53	0.33	0.77	14	empty

Interfaces

3 interfaces between chains.

B–C · 569 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 545 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 521 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1MST · Crystal structure of MS2 capsids with mutations in the subunit fg loop · the same entry in another collection · chain B against B, 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 P03612
Elsewhere: RCSB PDB 1MST · PDBe 1MST · UniProt P03612

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