MolNFT v1 · #6818 · protein
Crystal structure of N-acetylglucosaminyltransferase I
1FO8 · Alpha-1,3-mannosyl-glycoprotein beta-1,2-N…: “Crystal structure of N-acetylglucosaminyltransferase I”. X-ray diffraction, 1 ligand (MMC), 2 pockets (best druggability 0.54). MolNFT v1 #6818 on GenesisL1: 3D structure, binding sites…
- PDB
- 1FO8
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1,3-mannosyl-glycoprotein beta-1,2-N- acetylglucosaminyltransferase
- EC
- 2.4.1.101
- UniProt
- P27115
- Ligands
- MMC
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1,3-mannosyl-glycoprotein beta-1,2-N- acetylglucosaminyltransferase (EC 2.4.1.101) | protein | 330 | 35% helix, 22% strand | P27115 |
Ligands and binding sites
- MMC · Methyl mercury ion · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.54 | 0.77 | 37 | empty |
| 2 | 89 | 0.36 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P27115
- Elsewhere: RCSB PDB 1FO8 · PDBe 1FO8 · UniProt P27115
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