Research workbench
Crystal structure of C171A/V236A mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-valine
Analyse Crystal structure of C171A/V236A mutant of N-carbamyl-D-amino acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UF7
- Type
- protein
- Length
- 606 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-carbamyl-D-amino acid amidohydrolase
- EC
- 3.5.1.77
- UniProt
- P60327
- Ligands
- CDV
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-carbamyl-D-amino acid amidohydrolase (EC 3.5.1.77) | protein | 303 | 32% helix, 28% strand | P60327 |
Ligands and binding sites
- CDV · 3-methyl-2-ureido-butyric acid · ligand · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.79 | 0.93 | 37 | CDV |
| 2 | 283 | 0.79 | 0.91 | 42 | CDV |
| 3 | 61 | 0.28 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2573 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1UF7 · Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase… · the same entry in another collection · chain A against A, TM-score 1.00
- P60327 · AlphaFold monomer V2.0 prediction for N-carbamoyl-D-amino acid hydrolase (P60327) · 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 P60327
- Elsewhere: RCSB PDB 1UF7 · PDBe 1UF7 · UniProt P60327
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.