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Cryoem structure of recombinant CMV particles with tetanus-epitope

Analyse Cryoem structure of recombinant CMV particles with tetanus-epitope in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OW6
Type: protein
Length: 534 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VP1; Capsid protein, VP2; Capsid protein, VP3
UniProt: A0A1Q2SR16, K4TZS9
Pockets: 5 · best druggability 0.70

Structure

electron microscopy · 3 distinct chains · 10% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VP1	protein	153	8% helix, 25% strand	A0A1Q2SR16
B	Capsid protein, VP2	protein	190	11% helix, 25% strand	K4TZS9
C	Capsid protein, VP3	protein	191	11% helix, 25% strand	K4TZS9

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	857	0.70	0.76	66	empty
2	106	0.64	0.88	30	empty
3	306	0.52	0.74	47	empty
4	56	0.35	0.79	14	empty
5	54	0.24	0.72	12	empty

Interfaces

3 interfaces between chains.

B–C · 1232 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 809 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 383 Å² buried · 7 hydrogen bonds · protein-protein

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 A0A1Q2SR16
Every structure of UniProt K4TZS9
Elsewhere: RCSB PDB 5OW6 · PDBe 5OW6 · UniProt A0A1Q2SR16 · UniProt K4TZS9

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