Research workbench
Crystal structure of udp-N-acetylglucosamine 2-epimerase
Analyse Crystal structure of udp-N-acetylglucosamine 2-epimerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O6C
- Type
- protein
- Length
- 727 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine 2-epimerase
- EC
- 5.1.3.14
- UniProt
- P39131
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) | protein | 356 | 45% helix, 16% strand | P39131 |
| B | Udp-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) | protein | 371 | 47% helix, 16% strand | P39131 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 424 | 0.68 | 0.80 | 43 | empty |
| 2 | 337 | 0.56 | 0.75 | 46 | empty |
| 3 | 307 | 0.56 | 0.76 | 52 | empty |
| 4 | 65 | 0.35 | 0.77 | 13 | empty |
| 5 | 50 | 0.28 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1413 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 modified (engineered).
Compared structures
- 1O6C · Crystal structure of UDP-N-acetylglucosamine 2-epimerase · the same entry in another collection · chain A against A, TM-score 1.00
- P39131 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 2-epimerase (P39131) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P39131
- Elsewhere: RCSB PDB 1O6C · PDBe 1O6C · UniProt P39131
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