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Human cytomegalovirus, C12 portal

Analyse Human cytomegalovirus, C12 portal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ET2
Type: protein
Length: 4,812 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Portal protein
UniProt: Q6RXD3
Pockets: 20 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 48% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, G, J, E, H, K, F, I, L	Portal protein	protein	401	48% helix, 10% strand	Q6RXD3

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	183	0.75	0.91	27	empty
2	175	0.75	0.91	27	empty
3	167	0.74	0.91	28	empty
4	173	0.74	0.91	26	empty
5	81	0.74	0.97	22	empty

Interfaces

24 interfaces between chains.

I–L · 4815 Å² buried · 45 hydrogen bonds · protein-protein
G–J · 4810 Å² buried · 44 hydrogen bonds · protein-protein
H–K · 4810 Å² buried · 46 hydrogen bonds · protein-protein
B–C · 4807 Å² buried · 45 hydrogen bonds · protein-protein
K–F · 4790 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

7ET2 · Human Cytomegalovirus, C12 portal · 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 Q6RXD3
Elsewhere: RCSB PDB 7ET2 · PDBe 7ET2 · UniProt Q6RXD3

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