Research workbench
Structure of udp-galactopyranose mutase bound to udp-glucose
Analyse Structure of udp-galactopyranose mutase bound to udp-glucose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GF4
- Type
- protein
- Length
- 766 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-galactopyranose mutase
- EC
- 5.4.99.9
- UniProt
- Q48485
- Ligands
- FAD, UPG, U5P
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Udp-galactopyranose mutase (EC 5.4.99.9) | protein | 383 | 36% helix, 21% strand | Q48485 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- UPG · Uridine-5'-diphosphate-glucose · ligand · chains A
- U5P · Uridine-5'-monophosphate · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1092 | 0.84 | 0.85 | 103 | FAD, UPG |
| 2 | 1081 | 0.80 | 0.81 | 92 | FAD, U5P |
| 3 | 1074 | 0.76 | 0.78 | 68 | empty |
| 4 | 50 | 0.35 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1096 Ų buried · 13 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 Q48485
- Elsewhere: RCSB PDB 3GF4 · PDBe 3GF4 · UniProt Q48485
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