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MolNFT v1 · #119825 · protein

Crystal structure of human protein O-mannose beta-1,2-N- acetylglucosaminyltransferase form II

5GGF · Protein O-linked-mannose beta-1,2-N…: “Crystal structure of human protein O-mannose beta-1,2-N- acetylglucosaminyltransferase form II”. X-ray diffraction, 17 pockets (best druggability 0.71). MolNFT v1 #119825 on GenesisL1: 3D…

PDB
5GGF
Type
protein
Length
1,607 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein O-linked-mannose beta-1,2-N- acetylglucosaminyltransferase 1
EC
2.4.1.-
UniProt
Q8WZA1
Pockets
17 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein O-linked-mannose beta-1,2-N- acetylglucosaminyltransferase 1 (EC 2.4.1.-)protein53528% helix, 27% strandQ8WZA1
B, CProtein O-linked-mannose beta-1,2-N- acetylglucosaminyltransferase 1 (EC 2.4.1.-)protein53626% helix, 25% strandQ8WZA1

Pockets

17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17850.710.7778empty
27080.650.7479empty
33690.600.7647empty
43690.550.7440empty
52530.510.7534empty

Interfaces

3 interfaces between chains.

  • A–B · 729 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 348 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 240 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 disulfide (disulfide).

Compared structures

  • 5GGF · Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8WZA1 · AlphaFold monomer V2.0 prediction for protein O-linked-mannose… · a predicted model of the same protein · chain B against A, TM-score 0.97

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