MolNFT v1 · #98424 · protein
Crystal structure of gamma glutamyl hydrolase (H218N) from zebrafish
4L95 · Gamma-glutamyl hydrolase: “Crystal structure of gamma glutamyl hydrolase (H218N) from zebrafish”. X-ray diffraction, 20 pockets (best druggability 0.75). MolNFT v1 #98424 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4L95
- Type
- protein
- Length
- 1,722 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-glutamyl hydrolase
- EC
- 3.4.19.9
- UniProt
- Q6NY42
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F, C, G, K, M | Gamma-glutamyl hydrolase (EC 3.4.19.9) | protein | 287 | 36% helix, 27% strand | Q6NY42 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains C, G, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.75 | 0.97 | 23 | empty |
| 2 | 83 | 0.74 | 0.97 | 26 | empty |
| 3 | 60 | 0.73 | 0.98 | 19 | empty |
| 4 | 192 | 0.47 | 0.75 | 33 | empty |
| 5 | 186 | 0.47 | 0.75 | 38 | empty |
Interfaces
5 interfaces between chains.
- E–F · 1720 Ų buried · 10 hydrogen bonds · protein-protein
- C–G · 1697 Ų buried · 10 hydrogen bonds · protein-protein
- K–M · 1669 Ų buried · 10 hydrogen bonds · protein-protein
- G–M · 519 Ų buried · 3 hydrogen bonds · protein-protein
- E–C · 501 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4L95 · Crystal structure of gamma glutamyl hydrolase (H218N) from zebrafish · the same entry in another collection · chain E against E, 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 Q6NY42
- Elsewhere: RCSB PDB 4L95 · PDBe 4L95 · UniProt Q6NY42
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