MolNFT v1 · #91716 · protein
S-formylglutathione hydrolase W197I variant containing copper
4FLM: “S-formylglutathione hydrolase W197I variant containing copper”. X-ray diffraction, 1 ligand (CU), 3 pockets (best druggability 0.58). MolNFT v1 #91716 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4FLM
- Type
- protein
- Length
- 576 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
- P40363
- Ligands
- CU
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-formylglutathione hydrolase (EC 3.1.2.12) | protein | 288 | 35% helix, 24% strand | P40363 |
| B | S-formylglutathione hydrolase (EC 3.1.2.12) | protein | 288 | 36% helix, 22% strand | P40363 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A, 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.58 | 0.85 | 27 | empty |
| 2 | 89 | 0.40 | 0.77 | 20 | empty |
| 3 | 84 | 0.35 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 950 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard, oxidation).
Compared structures
- 4FLM · S-formylglutathione Hydrolase W197I Variant containing Copper · the same entry in another collection · chain A against A, TM-score 1.00
- P40363 · AlphaFold monomer V2.0 prediction for S-formylglutathione hydrolase (P40363) · a predicted model of the same protein · chain B 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 P40363
- Elsewhere: RCSB PDB 4FLM · PDBe 4FLM · UniProt P40363
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