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Neutron structure of human transthyretin (TTR) at room temperature to 2.0A resolution (Laue)

Analyse Neutron structure of human transthyretin (TTR) at room temperature to 2.0A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PVM
Type: protein
Length: 233 residues
Chains: 2
Method: neutron diffraction, x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.95,2
Source: Homo sapiens
Molecule: Transthyretin
UniProt: P02766
Pockets: 2 · best druggability 0.33

Structure

neutron diffraction, x-ray diffraction · resolution 1.95,2 · 2 distinct chains · 6% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	116	6% helix, 53% strand	P02766
B	Transthyretin	protein	117	6% helix, 52% strand	P02766

Pockets

2 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	72	0.33	0.76	15	empty
2	57	0.29	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 917 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

4PVM · Neutron structure of human transthyretin (ttr) at room temperature to 2.0A resolution… · 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 4PVM · PDBe 4PVM · UniProt P02766

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