Research workbench

Human Bocavirus 2 (pH 7.4)

Analyse Human Bocavirus 2 (pH 7.4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7L0V
Type: protein
Length: 30,360 residues
Chains: 60
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.71
Source: Human bocavirus 2
Molecule: VP2
UniProt: B9UYL6
Pockets: 20 · best druggability 0.79

Structure

electron microscopy · resolution 2.71 · 1 distinct chain · 9% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, t, u, v, w, x, y, z, 1, 2, 3, 4, 5, 6, 7, 8	VP2	protein	506	9% helix, 36% strand	B9UYL6

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	864	0.79	0.82	71	empty
2	952	0.79	0.81	74	empty
3	852	0.78	0.82	70	empty
4	1024	0.78	0.80	84	empty
5	1090	0.78	0.80	94	empty

Interfaces

150 interfaces between chains.

f–g · 4581 Å² buried · 75 hydrogen bonds · protein-protein
R–S · 4580 Å² buried · 75 hydrogen bonds · protein-protein
V–e · 4580 Å² buried · 75 hydrogen bonds · protein-protein
1–2 · 4580 Å² buried · 75 hydrogen bonds · protein-protein
T–l · 4580 Å² buried · 75 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 B9UYL6
Elsewhere: RCSB PDB 7L0V · PDBe 7L0V · UniProt B9UYL6

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