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Crystal structure of yfv-17D se in postfusion state

Analyse Crystal structure of yfv-17D se in postfusion state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IW1
Type: protein
Length: 1,132 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope protein E
UniProt: P03314
Pockets: 18 · best druggability 0.88

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Envelope protein E	protein	377	7% helix, 54% strand	P03314
B	Envelope protein E	protein	380	8% helix, 54% strand	P03314
C	Envelope protein E	protein	375	8% helix, 55% strand	P03314

Pockets

18 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1128	0.88	0.90	117	empty
2	364	0.72	0.84	50	empty
3	69	0.71	0.96	21	empty
4	429	0.69	0.81	50	empty
5	311	0.67	0.82	34	empty

Interfaces

3 interfaces between chains.

A–B · 2208 Å² buried · 28 hydrogen bonds · protein-protein
A–C · 2200 Å² buried · 28 hydrogen bonds · protein-protein
B–C · 2192 Å² buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

6IW1 · Crystal structure of YFV-17D sE in postfusion 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 P03314
Elsewhere: RCSB PDB 6IW1 · PDBe 6IW1 · UniProt P03314

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