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Human ALPHA2-macroglogulin is composed of multiple domains, as predicted by homology with complement component C3

Analyse Human ALPHA2-macroglogulin is composed of multiple domains, as predicted by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P9R
Type: protein
Length: 199 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P01023

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	102	—	P01023
B	—	protein	97	—	P01023

Compared structures

2P9R · Human alpha2-macroglogulin is composed of multiple domains, as predicted by homology with… · the same entry in another collection · chain B against B, TM-score 1.00
6TAV · Crystal structure of endopeptidase-induced ALPHA2-macroglobulin · an experimental structure of the same protein · chain B against B, TM-score 0.95
6TAV · Crystal structure of endopeptidase-induced alpha2-macroglobulin · an experimental structure of the same protein · chain B against B, TM-score 0.95
7O7Q · (H-ALPHA2M)4 trypsin-activated state · an experimental structure of the same protein · chain B against D, TM-score 0.95
7O7Q · (h-alpha2M)4 trypsin-activated state · an experimental structure of the same protein · chain B against D, TM-score 0.95

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 P01023
Elsewhere: RCSB PDB 2P9R · PDBe 2P9R · UniProt P01023 · AlphaFold DB P01023

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