Research workbench
Crystal structure of POFUT1 apo-form (crystal-form-I)
Analyse Crystal structure of POFUT1 apo-form (crystal-form-I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZY4
- Type
- protein
- Length
- 348 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative GDP-fucose protein O-fucosyltransferase 1
- EC
- 2.4.1.221
- UniProt
- Q18014
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative GDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) | protein | 348 | 42% helix, 15% strand | Q18014 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.58 | 0.80 | 30 | SO4 |
| 2 | 73 | 0.43 | 0.80 | 19 | empty |
| 3 | 103 | 0.38 | 0.75 | 27 | SO4 |
| 4 | 52 | 0.29 | 0.76 | 14 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3ZY4 · Crystal structure of POFUT1 apo-form (crystal-form-I) · the same entry in another collection · chain A against A, TM-score 1.00
- Q18014 · AlphaFold monomer V2.0 prediction for GDP-fucose protein O-fucosyltransferase 1 (Q18014) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q18014
- Elsewhere: RCSB PDB 3ZY4 · PDBe 3ZY4 · UniProt Q18014
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