MolNFT v1 · #163812 · protein

Transthyritin derived amyloid fibril from patient with hereditary V30M attr amyloidosis

6SDZ · Transthyretin: “Transthyritin derived amyloid fibril from patient with hereditary V30M attr amyloidosis”. Electron microscopy, 4 pockets (best druggability 0.86). MolNFT v1 #163812 on GenesisL1: 3D structure, binding sites and…

PDB: 6SDZ
Type: protein
Length: 1,012 residues
Chains: 11
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Pockets: 4 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 0% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K	Transthyretin	protein	92	0% helix, 53% strand	P02766

Pockets

4 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	843	0.86	0.89	99	empty
2	249	0.83	0.95	56	empty
3	267	0.80	0.92	62	empty
4	120	0.44	0.77	31	empty

Interfaces

19 interfaces between chains.

E–F · 3894 Å² buried · 128 hydrogen bonds · protein-protein
J–K · 3886 Å² buried · 141 hydrogen bonds · protein-protein
B–C · 3878 Å² buried · 131 hydrogen bonds · protein-protein
F–G · 3876 Å² buried · 130 hydrogen bonds · protein-protein
A–B · 3871 Å² buried · 140 hydrogen bonds · protein-protein

Compared structures

6SDZ · transthyritin derived amyloid fibril from patient with hereditary V30M ATTR amyloidosis · the same entry in another collection · chain A against A, TM-score 1.00

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 6SDZ · PDBe 6SDZ · UniProt P02766

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