Research workbench
Crystal structure of jack bean urease inhibited with fluoride
Analyse Crystal structure of jack bean urease inhibited with fluoride in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GOA
- Type
- protein
- Length
- 837 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Urease
- EC
- 3.5.1.5
- UniProt
- P07374
- Ligands
- NI, F
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Urease (EC 3.5.1.5) | protein | 837 | 30% helix, 23% strand | P07374 |
Ligands and binding sites
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 | 805 | 0.70 | 0.76 | 82 | empty |
| 2 | 146 | 0.43 | 0.75 | 16 | empty |
| 3 | 103 | 0.36 | 0.74 | 24 | empty |
| 4 | 75 | 0.30 | 0.73 | 17 | empty |
Modifications
Observed in the structure: 4 modified (artifact, carboxylation).
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 P07374
- Elsewhere: RCSB PDB 4GOA · PDBe 4GOA · UniProt P07374
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