Research workbench

Crystal structure of V30M mutant human transthyretin complexed with caffeic acid ethyl ester

Analyse Crystal structure of V30M mutant human transthyretin complexed with caffeic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PWG
Type: protein
Length: 231 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: 0XR, CA
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	116	5% helix, 53% strand	P02766
B	Transthyretin	protein	115	6% helix, 53% strand	P02766

Ligands and binding sites

0XR · ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	92	0.36	0.75	17	empty
2	56	0.29	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 923 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

4PWG · Crystal structure of V30M mutant human transthyretin complexed with caffeic acid ethyl… · 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 4PWG · PDBe 4PWG · UniProt P02766

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.