MolNFT v1 · #29990 · protein
Crystal structure of FET3P, a multicopper oxidase that functions in iron import
1ZPU · Iron transport multicopper oxidase FET3: “Crystal structure of FET3P, a multicopper oxidase that functions in iron import”. X-ray diffraction, 4 ligands (NAG, MAN, BMA), 20 pockets (best druggability 0.60). MolNFT v1 #29990 on…
- PDB
- 1ZPU
- Type
- protein
- Length
- 3,174 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron transport multicopper oxidase FET3
- EC
- 1.-.-.-
- UniProt
- P38993
- Ligands
- NAG, MAN, BMA, CU1
- Pockets
- 20 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Iron transport multicopper oxidase FET3 (EC 1.-.-.-) | protein | 529 | 11% helix, 38% strand | P38993 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 95 copies · chains A, B, C, D, E, F
- MAN · alpha-D-mannopyranose · sugar · 45 copies · chains A, B, C, D, E, F
- BMA · beta-D-mannopyranose · sugar · 26 copies · chains A, B, C, D, E, F
- CU1 · Copper (I) ion · metal · 24 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.60 | 0.78 | 37 | empty |
| 2 | 274 | 0.59 | 0.78 | 25 | empty |
| 3 | 251 | 0.59 | 0.79 | 26 | empty |
| 4 | 248 | 0.58 | 0.79 | 26 | empty |
| 5 | 255 | 0.58 | 0.78 | 28 | empty |
Interfaces
6 interfaces between chains.
- B–D · 476 Ų buried · 4 hydrogen bonds · protein-protein
- D–F · 467 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 329 Ų buried · 3 hydrogen bonds · protein-protein
- C–E · 328 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 327 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 63 glycan, 6 disulfide (N-glycosylation, disulfide).
Compared structures
- 1ZPU · Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import · the same entry in another collection · chain F against F, TM-score 1.00
- P38993 · AlphaFold monomer V2.0 prediction for iron transport multicopper oxidase FET3 (P38993) · a predicted model of the same protein · 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 P38993
- Elsewhere: RCSB PDB 1ZPU · PDBe 1ZPU · UniProt P38993
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.