Research workbench
Crystal structure of human renalase (isoform 1)
Analyse Crystal structure of human renalase (isoform 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QJ4
- Type
- protein
- Length
- 668 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Renalase
- EC
- 1.4.-.-
- UniProt
- Q5VYX0
- Ligands
- FAD, SO4
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Renalase (EC 1.4.-.-) | protein | 335 | 29% helix, 27% strand | Q5VYX0 |
| B | Renalase (EC 1.4.-.-) | protein | 333 | 29% helix, 28% strand | Q5VYX0 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 874 | 0.78 | 0.81 | 73 | FAD |
| 2 | 794 | 0.78 | 0.81 | 70 | FAD |
| 3 | 138 | 0.58 | 0.83 | 33 | empty |
| 4 | 185 | 0.42 | 0.73 | 22 | empty |
| 5 | 76 | 0.36 | 0.75 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 100 Ų buried · 1 hydrogen bond · protein-protein
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 Q5VYX0
- Elsewhere: RCSB PDB 3QJ4 · PDBe 3QJ4 · UniProt Q5VYX0
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