MolNFT v2 · #37351 · protein
Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in complex with Mn and UDP-galactose in open conformation
2FYB · Beta-1,4-galactosyltransferase 1: “Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in complex…”. X-ray diffraction at 1.9, 2 ligands (UDP, MN), 2 pockets (best druggability 0.55).…
- PDB
- 2FYB
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Homo sapiens
- Molecule
- Beta-1,4-galactosyltransferase 1
- EC
- 2.4.1.90
- UniProt
- P15291
- Ligands
- UDP, MN
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 24% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-1,4-galactosyltransferase 1 (EC 2.4.1.90) | protein | 272 | 24% helix, 22% strand | P15291 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 280 | 0.55 | 0.76 | 33 | MN, UDP |
| 2 | 63 | 0.51 | 0.87 | 21 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2FYB · Crystal structure of the catalytic domain of the human BETA1,4- galactosyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
- P15291 · AlphaFold monomer V2.0 prediction for beta-1,4-galactosyltransferase 1 (P15291) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P15291
- Elsewhere: RCSB PDB 2FYB · PDBe 2FYB · UniProt P15291
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