MolNFT v1 · #113612 · protein
X-ray structure and mutagenesis studies of the N- isopropylammelide isopropylaminohydrolase, atzc
5AKQ · N-isopropylammelide isopropyl amidohydrolase: “X-ray structure and mutagenesis studies of the N- isopropylammelide isopropylaminohydrolase, atzc”. X-ray diffraction, 2 ligands (ZN, CL), 5 pockets (best druggability 0.65). MolNFT v1…
- PDB
- 5AKQ
- Type
- protein
- Length
- 800 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-isopropylammelide isopropyl amidohydrolase
- EC
- 3.5.99.4
- UniProt
- O52063
- Ligands
- ZN, CL
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-isopropylammelide isopropyl amidohydrolase (EC 3.5.99.4) | protein | 400 | 37% helix, 24% strand | O52063 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.65 | 0.78 | 31 | empty |
| 2 | 189 | 0.57 | 0.80 | 30 | empty |
| 3 | 190 | 0.56 | 0.80 | 31 | empty |
| 4 | 114 | 0.45 | 0.78 | 32 | empty |
| 5 | 123 | 0.44 | 0.77 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 1965 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 5AKQ · X-ray structure and mutagenesis studies of the N-isopropylammelide… · the same entry in another collection · chain A against A, TM-score 1.00
- O52063 · AlphaFold monomer V2.0 prediction for N-isopropylammelide isopropyl amidohydrolase… · a predicted model of the same protein · chain A 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 O52063
- Elsewhere: RCSB PDB 5AKQ · PDBe 5AKQ · UniProt O52063
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