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Human myelin P2 mutant V115A

Analyse Human myelin P2 mutant V115A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NTP
Type: protein
Length: 265 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myelin P2 protein
UniProt: P02689
Ligands: PLM
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myelin P2 protein	protein	133	11% helix, 56% strand	P02689
B	Myelin P2 protein	protein	132	11% helix, 58% strand	P02689

Ligands and binding sites

PLM · Palmitic acid · ligand · 2 copies · chains A, B

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

Pockets

3 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	303	0.83	0.93	36	PLM
2	352	0.81	0.91	36	PLM
3	130	0.76	0.95	30	empty

Interfaces

1 interface between chains.

A–B · 619 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7NTP · Human myelin P2 mutant V115A · 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 7NTP · PDBe 7NTP · UniProt P02689

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