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Rat transthyretin

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

PDB: 1GKE
Type: protein
Length: 480 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02767
Pockets: 5 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transthyretin	protein	120	7% helix, 45% strand	P02767

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	421	0.72	0.82	47	empty
2	383	0.68	0.81	46	empty
3	66	0.34	0.76	15	empty
4	66	0.34	0.77	16	empty
5	73	0.33	0.75	16	empty

Interfaces

6 interfaces between chains.

C–D · 937 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 932 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 359 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 350 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 347 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

1GKE · Rat transthyretin · the same entry in another collection · chain A against A, TM-score 1.00
P02767 · AlphaFold monomer V2.0 prediction for transthyretin (P02767) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P02767
Elsewhere: RCSB PDB 1GKE · PDBe 1GKE · UniProt P02767

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