Research workbench

Structure of the BETA2_MICROGLOBULIN involved in amyloidogenesis

Analyse Structure of the BETA2_MICROGLOBULIN involved in amyloidogenesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X89
Type: protein
Length: 744 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P61769

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	—	protein	128	—	—
D	—	protein	92	—	P61769
E, F	—	protein	91	—	P61769
G	—	protein	86	—	P61769

Compared structures

2X89 · Structure of the Beta2_microglobulin involved in amyloidogenesis · the same entry in another collection · chain G against G, TM-score 1.00
P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain E against A, TM-score 0.77

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 P61769
Elsewhere: RCSB PDB 2X89 · PDBe 2X89 · UniProt P61769

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