MolNFT v1 · #148008 · protein

The fibrinogen-like domain of human ANGPTL3

6EUA · Angiopoietin-related protein 3: “The fibrinogen-like domain of human ANGPTL3”. X-ray diffraction, 3 pockets (best druggability 0.72). MolNFT v1 #148008 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6EUA
Type: protein
Length: 601 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Angiopoietin-related protein 3
UniProt: Q9Y5C1
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 3 distinct chains · 13% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Angiopoietin-related protein 3	protein	202	13% helix, 41% strand	Q9Y5C1
B	Angiopoietin-related protein 3	protein	201	13% helix, 40% strand	Q9Y5C1
C	Angiopoietin-related protein 3	protein	198	13% helix, 39% strand	Q9Y5C1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	880	0.72	0.77	113	empty
2	558	0.70	0.79	42	empty
3	54	0.30	0.76	12	empty

Interfaces

3 interfaces between chains.

A–C · 533 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 533 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 499 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

6EUA · The fibrinogen-like domain of human Angptl3 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y5C1 · AlphaFold monomer V2.0 prediction for angiopoietin-related protein 3 (Q9Y5C1) · a predicted model of the same protein · chain B 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 Q9Y5C1
Elsewhere: RCSB PDB 6EUA · PDBe 6EUA · UniProt Q9Y5C1

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