Research workbench
Crystal structure of TRX4 domain of ERDJ5
Analyse Crystal structure of TRX4 domain of ERDJ5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3APS
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dnaj homolog subfamily C member 10
- UniProt
- Q9DC23
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dnaj homolog subfamily C member 10 | protein | 114 | 42% helix, 25% strand | Q9DC23 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 376 | 0.57 | 0.75 | 42 | empty |
| 2 | 51 | 0.27 | 0.74 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 99 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q9DC23
- Elsewhere: RCSB PDB 3APS · PDBe 3APS · UniProt Q9DC23
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