Research workbench
Crystal structure of D-glucuronyl C5 epimerase
Analyse Crystal structure of D-glucuronyl C5 epimerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PW2
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-glucuronyl C5 epimerase B
- EC
- 5.1.3.17
- UniProt
- Q6TS32
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-glucuronyl C5 epimerase B (EC 5.1.3.17) | protein | 510 | 32% helix, 27% strand | Q6TS32 |
Ligands and binding sites
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.64 | 0.80 | 38 | CIT |
| 2 | 224 | 0.59 | 0.80 | 41 | empty |
| 3 | 58 | 0.36 | 0.79 | 12 | empty |
| 4 | 78 | 0.35 | 0.76 | 16 | empty |
| 5 | 66 | 0.31 | 0.75 | 18 | empty |
Compared structures
- 4PW2 · Crystal structure of D-glucuronyl C5 epimerase · 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 Q6TS32
- Elsewhere: RCSB PDB 4PW2 · PDBe 4PW2 · UniProt Q6TS32
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