MolNFT v1 · #51993 · protein
Crystal structure of the membrane proximal oxidoreductase domain of human STEAP3, the dominant ferric reductase of the erythroid transferrin cycle
2VNS · Metalloreductase STEAP3: “Crystal structure of the membrane proximal oxidoreductase domain of human STEAP3, the dominant ferric…”. X-ray diffraction, 4 pockets (best druggability 0.54). MolNFT v1 #51993 on GenesisL1: 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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