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Crystal structure analysis of norwalk virus capsid

Analyse Crystal structure analysis of norwalk virus capsid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IHM
Type: protein
Length: 1,495 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: Q83884
Pockets: 10 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Capsid protein	protein	492	8% helix, 34% strand	Q83884
B	Capsid protein	protein	511	9% helix, 32% strand	Q83884

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	802	0.86	0.88	90	empty
2	580	0.76	0.82	94	empty
3	567	0.74	0.82	53	empty
4	634	0.71	0.78	82	empty
5	141	0.70	0.90	32	empty

Interfaces

3 interfaces between chains.

A–B · 2420 Å² buried · 28 hydrogen bonds · protein-protein
B–C · 2007 Å² buried · 29 hydrogen bonds · protein-protein
A–C · 985 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1IHM · Crystal structure analysis of norwalk virus capsid · the same entry in another collection · chain C against C, 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 Q83884
Elsewhere: RCSB PDB 1IHM · PDBe 1IHM · UniProt Q83884

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