Research workbench
Crystal structure of the membrane proximal oxidoreductase domain of human STEAP3, the dominant ferric reductase of the erythroid transferrin cycle
Analyse Crystal structure of the membrane proximal oxidoreductase domain of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VNS
- Type
- protein
- Length
- 360 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metalloreductase STEAP3
- EC
- 1.16.1.2
- UniProt
- Q658P3
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Metalloreductase STEAP3 (EC 1.16.1.2) | protein | 180 | 43% helix, 22% strand | Q658P3 |
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
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.54 | 0.78 | 39 | empty |
| 2 | 216 | 0.52 | 0.77 | 38 | empty |
| 3 | 105 | 0.36 | 0.75 | 20 | empty |
| 4 | 97 | 0.35 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 734 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2VNS · Crystal Structure of the Membrane Proximal Oxidoreductase Domain of Human Steap3, the… · the same entry in another collection · chain A against A, TM-score 1.00
- Q658P3 · AlphaFold monomer V2.0 prediction for metalloreductase STEAP3 (Q658P3) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q658P3
- Elsewhere: RCSB PDB 2VNS · PDBe 2VNS · UniProt Q658P3
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