Research workbench
Crystal structure of escherichia COLI udp-galactose 4-epimerase mutant Y299C complexed with udp-N-acetylglucosamine
Analyse Crystal structure of escherichia COLI udp-galactose 4-epimerase mutant Y299C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LRK
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glucose 4-epimerase
- EC
- 5.1.3.2
- UniProt
- P09147
- Ligands
- NAD, UD1, NA
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glucose 4-epimerase (EC 5.1.3.2) | protein | 338 | 41% helix, 17% strand | P09147 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- PGE · Triethylene glycol · additive · 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 | 993 | 0.83 | 0.84 | 85 | NAD, UD1 |
| 2 | 142 | 0.59 | 0.84 | 25 | empty |
Compared structures
- 1LRK · Crystal Structure of Escherichia coli UDP-Galactose 4-Epimerase Mutant Y299C Complexed… · the same entry in another collection · chain A against A, TM-score 1.00
- P09147 · AlphaFold monomer V2.0 prediction for udp-glucose 4-epimerase (P09147) · 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 P09147
- Elsewhere: RCSB PDB 1LRK · PDBe 1LRK · UniProt P09147
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