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Crystal structure of human apom in complex with myristic acid

Analyse Crystal structure of human apom in complex with myristic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WEW
Type: protein
Length: 170 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apolipoprotein M
UniProt: O95445
Ligands: MYR
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apolipoprotein M	protein	170	15% helix, 40% strand	O95445

Ligands and binding sites

MYR · Myristic acid · ligand · chains A
EDO · 1,2-ethanediol · additive · chains A

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

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	219	0.73	0.87	32	MYR
2	51	0.41	0.83	14	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2WEW · Crystal structure of human apoM in complex with myristic acid · the same entry in another collection · chain A against A, TM-score 1.00
O95445 · AlphaFold monomer V2.0 prediction for apolipoprotein M (O95445) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O95445
Elsewhere: RCSB PDB 2WEW · PDBe 2WEW · UniProt O95445

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