Research workbench
Crystal structure of oxidoreductase ROP_24000 (target efi-506400) from rhodococcus opacus B4
Analyse Crystal structure of oxidoreductase ROP_24000 (target efi-506400) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JXK
- Type
- protein
- Length
- 654 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxidoreductase
- EC
- 1.-.-.-
- UniProt
- C1B3E9
- Ligands
- CL
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Oxidoreductase (EC 1.-.-.-) | protein | 327 | 30% helix, 29% strand | C1B3E9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 688 | 0.76 | 0.81 | 65 | EDO |
| 2 | 720 | 0.75 | 0.81 | 66 | CL, EDO |
| 3 | 214 | 0.52 | 0.77 | 24 | empty |
| 4 | 174 | 0.50 | 0.78 | 25 | empty |
| 5 | 92 | 0.39 | 0.77 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1215 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 4JXK · Crystal Structure of Oxidoreductase ROP_24000 (Target EFI-506400) from Rhodococcus opacus… · 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 C1B3E9
- Elsewhere: RCSB PDB 4JXK · PDBe 4JXK · UniProt C1B3E9
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