MolNFT v1 · #112627 · protein
Full length SCS7P (only hydroxylase domain visible)
4ZR0 · Ceramide very long chain fatty acid hydroxylase SCS7: “Full length SCS7P (only hydroxylase domain visible)”. X-ray diffraction, 1 ligand (ZN), 10 pockets (best druggability 0.79). MolNFT v1 #112627 on GenesisL1: 3D structure…
- PDB
- 4ZR0
- Type
- protein
- Length
- 534 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ceramide very long chain fatty acid hydroxylase SCS7
- EC
- 1.-.-.-
- UniProt
- Q03529
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ceramide very long chain fatty acid hydroxylase SCS7 (EC 1.-.-.-) | protein | 264 | 58% helix, 0% strand | Q03529 |
| B | Ceramide very long chain fatty acid hydroxylase SCS7 (EC 1.-.-.-) | protein | 270 | 57% helix, 1% strand | Q03529 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 918 | 0.79 | 0.80 | 54 | empty |
| 2 | 610 | 0.73 | 0.80 | 68 | empty |
| 3 | 234 | 0.70 | 0.85 | 27 | empty |
| 4 | 159 | 0.67 | 0.86 | 26 | empty |
| 5 | 105 | 0.52 | 0.83 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 484 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4ZR0 · Full length scs7p (only hydroxylase domain visible) · the same entry in another collection · chain A against A, TM-score 1.00
- Q03529 · AlphaFold monomer V2.0 prediction for ceramide very long chain fatty acid hydroxylase… · 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 Q03529
- Elsewhere: RCSB PDB 4ZR0 · PDBe 4ZR0 · UniProt Q03529
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