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Structure of the catalytic domain of human endo-alpha-mannosidase manea in complex with nickel

Analyse Structure of the catalytic domain of human endo-alpha-mannosidase manea in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZDC
Type
protein
Length
350 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycoprotein endo-alpha-1,2-mannosidase
EC
3.2.1.130
UniProt
Q5SRI9
Ligands
NI
Pockets
4 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycoprotein endo-alpha-1,2-mannosidase (EC 3.2.1.130)protein35032% helix, 16% strandQ5SRI9

Ligands and binding sites

  • NI · Nickel (II) ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.540.7831empty
21840.440.7433empty
3580.350.7817empty
4510.270.7415empty

Compared structures

  • 6ZDC · Structure of the catalytic domain of human endo-alpha-mannosidase MANEA in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5SRI9 · AlphaFold monomer V2.0 prediction for glycoprotein endo- alpha-1,2-mannosidase (Q5SRI9) · a predicted model of the same protein · chain A against A, TM-score 0.98

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