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High resolution structure of human CD59

Analyse High resolution structure of human CD59 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2UX2
Type: protein
Length: 234 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.8
Source: HOMO SAPIENS
Molecule: CD59 glycoprotein
UniProt: P13987
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · resolution 1.8 · 1 distinct chain · 18% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	CD59 glycoprotein	protein	78	18% helix, 32% strand	P13987

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	440	0.64	0.78	52	empty
2	59	0.29	0.75	13	empty

Interfaces

3 interfaces between chains.

A–B · 244 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 230 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 94 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 15 disulfide (disulfide).

Compared structures

2UX2 · High resolution structure of human CD59 · the same entry in another collection · chain A against A, TM-score 1.00
P13987 · AlphaFold monomer V2.0 prediction for CD59 glycoprotein (P13987) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P13987
Elsewhere: RCSB PDB 2UX2 · PDBe 2UX2 · UniProt P13987

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