Research workbench
A20 otu domain in reversibly oxidised (soh) state
Analyse A20 otu domain in reversibly oxidised (soh) state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZJE
- Type
- protein
- Length
- 653 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- A20P50
- EC
- 3.4.19.12, 6.3.2.-
- UniProt
- P21580
- Ligands
- CL
- Pockets
- 6 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | A20P50 (EC 3.4.19.12, 6.3.2.-) | protein | 329 | 40% helix, 19% strand | P21580 |
| B | A20P50 (EC 3.4.19.12, 6.3.2.-) | protein | 324 | 38% helix, 19% strand | P21580 |
Ligands and binding sites
- CL · Chloride ion · ion · 6 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.58 | 0.82 | 35 | CL |
| 2 | 131 | 0.53 | 0.81 | 33 | CL |
| 3 | 67 | 0.41 | 0.80 | 14 | empty |
| 4 | 66 | 0.39 | 0.79 | 17 | empty |
| 5 | 65 | 0.38 | 0.79 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 687 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
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 P21580
- Elsewhere: RCSB PDB 3ZJE · PDBe 3ZJE · UniProt P21580
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