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Human myelin P2 protein, K112Q mutant

Analyse Human myelin P2 protein, K112Q mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4A8Z
Type: protein
Length: 133 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myelin P2 protein
UniProt: P02689
Ligands: PLM, SO4
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myelin P2 protein	protein	133	15% helix, 57% strand	P02689

Ligands and binding sites

PLM · Palmitic acid · ligand · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	285	0.82	0.93	36	PLM

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4A8Z · Human myelin P2 protein, K112Q mutant · the same entry in another collection · chain A against A, TM-score 1.00
P02689 · AlphaFold monomer V2.0 prediction for myelin P2 protein (P02689) · a predicted model of the same protein · chain A 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 P02689
Elsewhere: RCSB PDB 4A8Z · PDBe 4A8Z · UniProt P02689

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