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Structure of the catalytic domain of mouse manic fringe in complex with udp and manganese

Analyse Structure of the catalytic domain of mouse manic fringe in complex with udp and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2J0B
Type
protein
Length
243 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-1,3-N-acetylglucosaminyltransferase manic fringe
EC
2.4.1.222
UniProt
O09008
Ligands
UDP, K, MN, SO4

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-1,3-N-acetylglucosaminyltransferase manic fringe (EC 2.4.1.222)protein24339% helix, 19% strandO09008

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · chains A
  • K · Potassium ion · metal · chains A
  • MN · Manganese (II) ion · metal · chains A
  • SO4 · Sulfate ion · ion · chains A

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

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 2J0B · Structure of the catalytic domain of mouse Manic Fringe in complex with UDP and manganese · the same entry in another collection · chain A against A, TM-score 1.00
  • O09008 · AlphaFold monomer V2.0 prediction for beta-1,3-N-acetylglucosaminyltransferase manic… · a predicted model of the same protein · chain A against A, TM-score 0.96

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