MolNFT v1 · #91629 · protein
Crystal structure of GLFT2 complexed with udp
4FIY · Udp-galactofuranosyl transferase GLFT2: “Crystal structure of GLFT2 complexed with udp”. X-ray diffraction, 2 ligands (UDP, MN), 11 pockets (best druggability 0.79). MolNFT v1 #91629 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4FIY
- Type
- protein
- Length
- 1,256 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-galactofuranosyl transferase GLFT2
- EC
- 2.4.1.-
- UniProt
- O53585
- Ligands
- UDP, MN
- Pockets
- 11 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Udp-galactofuranosyl transferase GLFT2 (EC 2.4.1.-) | protein | 628 | 36% helix, 24% strand | O53585 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1048 | 0.79 | 0.81 | 77 | UDP, MN |
| 2 | 1040 | 0.78 | 0.80 | 77 | UDP, MN |
| 3 | 815 | 0.72 | 0.77 | 62 | empty |
| 4 | 313 | 0.57 | 0.76 | 50 | empty |
| 5 | 178 | 0.52 | 0.78 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 263 Ų buried · 0 hydrogen bonds · protein-protein
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 O53585
- Elsewhere: RCSB PDB 4FIY · PDBe 4FIY · UniProt O53585
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