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Crystal structure of AMUC_1102 from akkermansia muciniphila

Analyse Crystal structure of AMUC_1102 from akkermansia muciniphila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DSZ
Type
protein
Length
568 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
AMUC_1102
UniProt
B2UR43
Ligands
CL
Pockets
8 · best druggability 0.85

Structure

x-ray diffraction · 3 distinct chains · 11% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAMUC_1102protein18611% helix, 46% strandB2UR43
BAMUC_1102protein19011% helix, 45% strandB2UR43
CAMUC_1102protein19210% helix, 45% strandB2UR43

Ligands and binding sites

  • CL · Chloride ion · ion · 5 copies · chains A, B, C

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

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110700.850.86133empty
2520.660.9515empty
3940.510.8316empty
41490.490.7822empty
51400.440.7621empty

Interfaces

3 interfaces between chains.

  • A–B · 1517 Ų buried · 23 hydrogen bonds · protein-protein
  • B–C · 1488 Ų buried · 23 hydrogen bonds · protein-protein
  • A–C · 1294 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 7DSZ · Crystal structure of Amuc_1102 from Akkermansia muciniphila · the same entry in another collection · chain A against A, TM-score 1.00

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