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Crystal structure of the drosophila BETA1,4GALACTOSYLTRANSFERASE7 catalytic domain D211N single mutant enzyme complex with manganese and udp-galactose
Analyse Crystal structure of the drosophila BETA1,4GALACTOSYLTRANSFERASE7 catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LW3
- Type
- protein
- Length
- 242 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-4-galactosyltransferase 7
- EC
- 2.4.1.-, 2.4.1.133
- UniProt
- Q9VBZ9
- Ligands
- GDU, MN
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-4-galactosyltransferase 7 (EC 2.4.1.-, 2.4.1.133) | protein | 242 | 23% helix, 24% strand | Q9VBZ9 |
Ligands and binding sites
- GDU · Galactose-uridine-5'-diphosphate · ligand · chains A
- MN · Manganese (II) ion · metal · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.78 | 0.88 | 37 | MN, GDU |
| 2 | 130 | 0.53 | 0.81 | 22 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4LW3 · Crystal structure of the Drosophila beta1,4galactosyltransferase7 catalytic domain D211N… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9VBZ9
- Elsewhere: RCSB PDB 4LW3 · PDBe 4LW3 · UniProt Q9VBZ9
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