Research workbench
Crystal structure of udp-N-acetylglucosamine 2-epimerase from thermus thermophilus HB8
Analyse Crystal structure of udp-N-acetylglucosamine 2-epimerase from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V4V
- Type
- protein
- Length
- 745 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
- P83824
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) | protein | 373 | 47% helix, 15% strand | P83824 |
| B | Udp-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) | protein | 372 | 44% helix, 16% strand | P83824 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 506 | 0.65 | 0.77 | 59 | empty |
| 2 | 214 | 0.54 | 0.78 | 31 | empty |
| 3 | 203 | 0.50 | 0.76 | 28 | empty |
| 4 | 172 | 0.46 | 0.75 | 27 | GOL |
| 5 | 143 | 0.44 | 0.76 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1242 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 1V4V · Crystal Structure Of UDP-N-Acetylglucosamine 2-Epimerase From Thermus Thermophilus HB8 · 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 P83824
- Elsewhere: RCSB PDB 1V4V · PDBe 1V4V · UniProt P83824
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