GL1X · GenesisL1 explorer

MolNFT v1 · #183929 · protein

(H-ALPHA2M)4 native II

7O7M · Alpha-2-macroglobulin: “(H-ALPHA2M)4 native II”. Electron microscopy, 3 ligands (NAG, BMA, MAN), 20 pockets (best druggability 0.88). MolNFT v1 #183929 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7O7M
Type
protein
Length
5,640 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-2-macroglobulin
UniProt
P01023
Ligands
NAG, BMA, MAN
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 13% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DAlpha-2-macroglobulinprotein141013% helix, 24% strandP01023

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 38 copies · chains B, D, A, C
  • BMA · beta-D-mannopyranose · sugar · 4 copies
  • MAN · alpha-D-mannopyranose · sugar · 2 copies

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110130.880.89141empty
211810.860.87147empty
311030.860.87118empty
410830.860.87115empty
56610.860.9093empty

Interfaces

6 interfaces between chains.

  • A–D · 1002 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 996 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 653 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 652 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 451 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 48 disulfide, 30 glycan (disulfide, N-glycosylation).

Compared structures

  • 7O7M · (h-alpha2M)4 native II · the same entry in another collection · chain D against D, TM-score 1.00
  • P01023 · AlphaFold monomer V2.0 prediction for alpha-2-macroglobulin (P01023) · a predicted model of the same protein · chain D against A, TM-score 0.85
  • 2P9R · Human ALPHA2-macroglogulin is composed of multiple domains, as predicted by homology with… · a predicted model of the same protein · chain C against A, TM-score 0.07
  • 2P9R · Human alpha2-macroglogulin is composed of multiple domains, as predicted by homology with… · a predicted model of the same protein · chain A against A, TM-score 0.07

Analyse

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