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Crystal structure of mavirus major capsid protein

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

PDB: 6G45
Type: protein
Length: 1,509 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative major capsid protein
UniProt: A0A1L4BK98
Pockets: 18 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Putative major capsid protein	protein	503	14% helix, 38% strand	A0A1L4BK98

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

18 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	971	0.80	0.82	94	empty
2	480	0.76	0.84	51	empty
3	472	0.76	0.84	45	empty
4	556	0.73	0.82	65	empty
5	450	0.69	0.80	54	empty

Interfaces

3 interfaces between chains.

A–B · 3853 Å² buried · 48 hydrogen bonds · protein-protein
A–C · 3851 Å² buried · 48 hydrogen bonds · protein-protein
B–C · 3850 Å² buried · 46 hydrogen bonds · protein-protein

Compared structures

6G45 · Crystal structure of mavirus major capsid 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 A0A1L4BK98
Elsewhere: RCSB PDB 6G45 · PDBe 6G45 · UniProt A0A1L4BK98

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