MolNFT v1 · #63546 · protein
Crystal structure of human esterase D
3FCX · S-formylglutathione hydrolase: “Crystal structure of human esterase D”. X-ray diffraction, 2 ligands (CA, MG), 6 pockets (best druggability 0.81). MolNFT v1 #63546 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FCX
- Type
- protein
- Length
- 543 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-formylglutathione hydrolase
- EC
- 3.1.2.12
- UniProt
- P10768
- Ligands
- CA, MG
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-formylglutathione hydrolase (EC 3.1.2.12) | protein | 268 | 38% helix, 25% strand | P10768 |
| B | S-formylglutathione hydrolase (EC 3.1.2.12) | protein | 275 | 36% helix, 23% strand | P10768 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 601 | 0.81 | 0.86 | 67 | empty |
| 2 | 85 | 0.49 | 0.83 | 22 | empty |
| 3 | 123 | 0.46 | 0.78 | 15 | empty |
| 4 | 60 | 0.33 | 0.76 | 15 | empty |
| 5 | 50 | 0.30 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 908 Ų buried · 9 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 P10768
- Elsewhere: RCSB PDB 3FCX · PDBe 3FCX · UniProt P10768
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