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Leu 55 pro transthyretin crystal structure

Analyse Leu 55 pro transthyretin crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TTR
Type: protein
Length: 928 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Pockets: 9 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Transthyretin	protein	116	5% helix, 53% strand	P02766

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	403	0.73	0.84	60	empty
2	593	0.68	0.78	43	empty
3	284	0.67	0.83	40	empty
4	492	0.59	0.74	49	empty
5	152	0.50	0.78	16	empty

Interfaces

14 interfaces between chains.

E–F · 920 Å² buried · 18 hydrogen bonds · protein-protein
G–H · 897 Å² buried · 20 hydrogen bonds · protein-protein
C–D · 896 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 895 Å² buried · 15 hydrogen bonds · protein-protein
D–F · 393 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5TTR · Leu 55 pro transthyretin crystal structure · 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 5TTR · PDBe 5TTR · UniProt P02766

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