Research workbench

Structure of HSV2 viron capsid portal vertex

Analyse Structure of HSV2 viron capsid portal vertex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6M6G
Type: protein
Length: 10,590 residues
Chains: 22
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major capsid protein; Small capsomere-interacting protein; Triplex capsid protein 2…
EC: 3.4.19.12, 3.4.22.-
UniProt: P89442, G9I257, G9I239, G9I260, P89440, P89448, P89459
Pockets: 20 · best druggability 0.88

Structure

electron microscopy · 14 distinct chains · 30% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, C, D	Major capsid protein	protein	1362	29% helix, 12% strand	P89442
E	Major capsid protein	protein	1351	27% helix, 15% strand	P89442
F	Major capsid protein	protein	1351	28% helix, 12% strand	P89442
G, M, Q, T, U, V	Small capsomere-interacting protein	protein	101	31% helix, 0% strand	G9I257
I	Major capsid protein	protein	1319	28% helix, 10% strand	P89442
K	Triplex capsid protein 2	protein	299	33% helix, 16% strand	G9I239
L	Coiled coils	protein	84	92% helix, 0% strand	—
O	Triplex capsid protein 2	protein	307	25% helix, 18% strand	G9I239
P	Coiled coils	protein	87	79% helix, 0% strand	—
S	Triplex capsid protein 1	protein	279	19% helix, 14% strand	G9I260
k	Capsid vertex component 1	protein	553	34% helix, 17% strand	P89440
l	Capsid vertex component 2	protein	94	33% helix, 4% strand	P89448
m	Capsid vertex component 2	protein	80	41% helix, 1% strand	P89448
n, o	Large tegument protein deneddylase (EC 3.4.19.12, 3.4.22.-)	protein	47	60% helix, 0% strand	P89459

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	1058	0.88	0.89	161	empty
2	1039	0.87	0.88	136	empty
3	692	0.86	0.91	94	empty
4	531	0.86	0.92	79	empty
5	512	0.86	0.92	79	empty

Interfaces

47 interfaces between chains.

B–I · 6078 Å² buried · 68 hydrogen bonds · protein-protein
C–D · 6034 Å² buried · 67 hydrogen bonds · protein-protein
D–E · 6021 Å² buried · 67 hydrogen bonds · protein-protein
B–C · 5878 Å² buried · 61 hydrogen bonds · protein-protein
E–F · 5835 Å² buried · 65 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

6M6G · Structure of HSV2 viron capsid portal vertex · 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 P89442
Every structure of UniProt G9I257
Every structure of UniProt G9I239
Every structure of UniProt G9I260
Every structure of UniProt P89440
Every structure of UniProt P89448
Every structure of UniProt P89459
Elsewhere: RCSB PDB 6M6G · PDBe 6M6G · UniProt P89442 · UniProt G9I257 · UniProt G9I239 · UniProt G9I260 · UniProt P89440 · UniProt P89448 · UniProt P89459

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.