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Crystal structure of yfv-china se in prefusion state

Analyse Crystal structure of yfv-china se in prefusion state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IW5
Type: protein
Length: 1,572 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope protein
UniProt: Q89292
Pockets: 9 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Envelope protein	protein	393	9% helix, 51% strand	Q89292

Pockets

9 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	968	0.73	0.77	78	empty
2	149	0.70	0.89	23	empty
3	613	0.69	0.78	61	empty
4	181	0.48	0.76	28	empty
5	176	0.47	0.75	22	empty

Interfaces

5 interfaces between chains.

B–D · 566 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 438 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 249 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 106 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 62 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 disulfide (disulfide).

Compared structures

6IW5 · Crystal structure of YFV-China sE in prefusion state · 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 Q89292
Elsewhere: RCSB PDB 6IW5 · PDBe 6IW5 · UniProt Q89292

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