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Crystal Structure of Evasin-1

Analyse Crystal Structure of Evasin-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FPR
Type: protein
Length: 163 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.63
Source: Rhipicephalus sanguineus
Molecule: Evasin-1
UniProt: P0C8E7
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · resolution 1.63 · 2 distinct chains · 8% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Evasin-1	protein	85	8% helix, 47% strand	P0C8E7
D	Evasin-1	protein	78	8% helix, 49% strand	P0C8E7

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.35	0.73	20	empty
2	60	0.24	0.72	18	empty

Interfaces

1 interface between chains.

A–D · 905 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

3FPR · Crystal structure of evasin-1 · the same entry in another collection · chain A against A, TM-score 1.00
P0C8E7 · AlphaFold monomer V2.0 prediction for evasin-1 (P0C8E7) · a predicted model of the same protein · chain D against A, TM-score 0.95

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 P0C8E7
Elsewhere: RCSB PDB 3FPR · PDBe 3FPR · UniProt P0C8E7

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