MolNFT v1 · #15265 · protein
QR15, an aldolase
1MZH · Deoxyribose-phosphate aldolase: “QR15, an aldolase”. X-ray diffraction, 1 ligand (PO4), 3 pockets (best druggability 0.57). MolNFT v1 #15265 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MZH
- Type
- protein
- Length
- 446 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxyribose-phosphate aldolase
- EC
- 4.1.2.4
- UniProt
- O66540
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxyribose-phosphate aldolase (EC 4.1.2.4) | protein | 225 | 48% helix, 16% strand | O66540 |
| B | Deoxyribose-phosphate aldolase (EC 4.1.2.4) | protein | 221 | 50% helix, 17% strand | O66540 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.57 | 0.79 | 42 | empty |
| 2 | 143 | 0.56 | 0.82 | 24 | PO4 |
| 3 | 62 | 0.29 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1635 Ų buried · 19 hydrogen bonds · 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 O66540
- Elsewhere: RCSB PDB 1MZH · PDBe 1MZH · UniProt O66540
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