Research workbench

Human angiopoietin-like 4 C-terminal domain (CANGPTL4) with myristic acid

Analyse Human angiopoietin-like 4 C-terminal domain (CANGPTL4) 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: 6U73
Type: protein
Length: 216 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Angiopoietin-related protein 4
UniProt: Q9BY76
Ligands: MYR
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Angiopoietin-related protein 4	protein	216	19% helix, 32% strand	Q9BY76

Ligands and binding sites

MYR · Myristic acid · ligand · 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	149	0.69	0.88	21	MYR

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6U73 · Human Angiopoietin-Like 4 C-Terminal Domain (cANGPTL4) with Myristic Acid · the same entry in another collection · chain A against A, TM-score 1.00
Q9BY76 · AlphaFold monomer V2.0 prediction for angiopoietin-related protein 4 (Q9BY76) · 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 Q9BY76
Elsewhere: RCSB PDB 6U73 · PDBe 6U73 · UniProt Q9BY76

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