Research workbench
Zn-binding domain of the T347G mutant of human aminoacylase-I
Analyse Zn-binding domain of the T347G mutant of human aminoacylase-I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q7L
- Type
- protein
- Length
- 555 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminoacylase-1
- EC
- 3.5.1.14
- UniProt
- Q03154
- Ligands
- GLY, ZN
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminoacylase-1 (EC 3.5.1.14) | protein | 192 | 30% helix, 24% strand | Q03154 |
| B | Aminoacylase-1 (EC 3.5.1.14) | protein | 88 | 47% helix, 14% strand | Q03154 |
| C | Aminoacylase-1 (EC 3.5.1.14) | protein | 190 | 31% helix, 24% strand | Q03154 |
| D | Aminoacylase-1 (EC 3.5.1.14) | protein | 85 | 45% helix, 14% strand | Q03154 |
Ligands and binding sites
- GLY · Glycine · ligand · 2 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 853 | 0.84 | 0.87 | 88 | GLY |
| 2 | 73 | 0.38 | 0.77 | 19 | empty |
| 3 | 68 | 0.35 | 0.77 | 18 | empty |
| 4 | 52 | 0.33 | 0.78 | 13 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3578 Ų buried · 71 hydrogen bonds · protein-protein
- C–D · 3531 Ų buried · 67 hydrogen bonds · protein-protein
- A–C · 513 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 357 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 306 Ų buried · 2 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 Q03154
- Elsewhere: RCSB PDB 1Q7L · PDBe 1Q7L · UniProt Q03154
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