Research workbench
Rat metallophosphodiesterase MPPED2 H67R mutant
Analyse Rat metallophosphodiesterase MPPED2 H67R mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RL5
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallophosphoesterase MPPED2
- EC
- 3.1.-.-
- UniProt
- B1WBP0
- Ligands
- CA, NO3
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metallophosphoesterase MPPED2 (EC 3.1.-.-) | protein | 279 | 26% helix, 22% strand | B1WBP0 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
- NO3 · Nitrate 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
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.45 | 0.75 | 27 | CA |
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 3RL5 · PDBe 3RL5 · UniProt B1WBP0
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