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Crystal structure of the transthyretin mutant A108Y/L110E solved in space group C2

Analyse Crystal structure of the transthyretin mutant A108Y/L110E solved in space group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SOQ
Type: protein
Length: 462 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Pockets: 4 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Transthyretin	protein	116	6% helix, 49% strand	P02766
B, D	Transthyretin	protein	115	6% helix, 51% strand	P02766

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	118	0.46	0.78	15	empty
2	137	0.44	0.76	21	empty
3	75	0.39	0.78	18	empty
4	52	0.27	0.74	11	empty

Interfaces

4 interfaces between chains.

C–D · 906 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 335 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 248 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 145 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1SOQ · Crystal structure of the transthyretin mutant A108Y/L110E solved in space group C2 · 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 1SOQ · PDBe 1SOQ · UniProt P02766

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