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Serial femtosecond X-ray structure of a stem domain of human O-mannose beta-1,2-N-acetylglucosaminyltransferase solved by se-sad using xfel (refined against 13,000 patterns)

Analyse Serial femtosecond X-ray structure of a stem domain of human O-mannose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XFC
Type
protein
Length
306 residues
Chains
2
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
Ligands
MBE
Pockets
2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProtein O-linked-mannose beta-1,2-N- acetylglucosaminyltransferase 1 (EC 2.4.1.-)protein15315% helix, 41% strandQ8WZA1

Ligands and binding sites

  • MBE · 4-nitrophenyl beta-D-mannopyranoside · ligand · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12390.500.7537empty
2520.370.8014empty

Interfaces

1 interface between chains.

  • A–B · 481 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 5XFC · Serial femtosecond X-ray structure of a stem domain of human O-mannose… · 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 A against A, TM-score 0.99

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