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Structure of american mink ACE2

Analyse Structure of american mink ACE2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7WA3
Type
protein
Length
1,200 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Angiotensin-converting enzyme
EC
3.4.-.-
UniProt
A0A7T0Q2W2
Ligands
NAG, FUC, ZN
Pockets
7 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAngiotensin-converting enzyme (EC 3.4.-.-)protein60062% helix, 4% strandA0A7T0Q2W2

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains B, A
  • FUC · alpha-L-fucopyranose · sugar
  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19070.710.7670empty
26740.690.7753empty
37610.670.7573empty
44730.670.7841empty
54950.660.7845empty

Interfaces

1 interface between chains.

  • A–B · 234 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 5 glycan (disulfide, N-glycosylation).

Compared structures

  • 7WA3 · Structure of American mink ACE2 · the same entry in another collection · chain A against A, TM-score 1.00

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