MolNFT v2 · #223057 · protein

Unliganded human transthyretin in the canonical conformation

8VE2: “Unliganded human transthyretin in the canonical conformation”. Electron microscopy at 3.3, 4 pockets (best druggability 0.80). MolNFT v2 #223057 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 8VE2
Type: protein
Length: 465 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.3
Source: Homo sapiens
Molecule: Transthyretin
UniProt: P02766
Pockets: 4 · best druggability 0.80

Structure

electron microscopy · resolution 3.3 · 3 distinct chains · 7% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transthyretin	protein	117	7% helix, 49% strand	P02766
C	Transthyretin	protein	116	6% helix, 53% strand	P02766
D	Transthyretin	protein	115	7% helix, 46% strand	P02766

Pockets

4 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	709	0.80	0.84	93	empty
2	71	0.37	0.77	17	empty
3	78	0.33	0.74	15	empty
4	52	0.27	0.74	14	empty

Interfaces

6 interfaces between chains.

A–B · 832 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 795 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 306 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 296 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 290 Å² buried · 2 hydrogen bonds · protein-protein

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 P02766
Elsewhere: RCSB PDB 8VE2 · PDBe 8VE2 · UniProt P02766

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