MolNFT v1 · #77644 · protein
Rat metallophosphodiesterase MPPED2 G252H mutant
3RL4 · Metallophosphoesterase MPPED2: “Rat metallophosphodiesterase MPPED2 G252H mutant”. X-ray diffraction, 3 ligands (5GP, MN, CL), 2 pockets (best druggability 0.53). MolNFT v1 #77644 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3RL4
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallophosphoesterase MPPED2
- EC
- 3.1.-.-
- UniProt
- B1WBP0
- Ligands
- 5GP, MN, CL
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metallophosphoesterase MPPED2 (EC 3.1.-.-) | protein | 275 | 24% helix, 23% strand | B1WBP0 |
Ligands and binding sites
- 5GP · Guanosine-5'-monophosphate · ligand · chains A
- MN · Manganese (II) ion · metal · 8 copies · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.53 | 0.78 | 32 | 5GP |
| 2 | 51 | 0.33 | 0.78 | 14 | EDO |
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 B1WBP0
- Elsewhere: RCSB PDB 3RL4 · PDBe 3RL4 · UniProt B1WBP0
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