Research workbench
Crystal structure of ohcu decarboxylase in the presence of (S)-allantoin
Analyse Crystal structure of ohcu decarboxylase in the presence of (S)-allantoin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q37
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ohcu decarboxylase
- UniProt
- Q9LVM5
- Ligands
- 3AL
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ohcu decarboxylase | protein | 142 | 64% helix, 0% strand | Q9LVM5 |
Ligands and binding sites
- 3AL · 1-[(4S)-2,5-dioxoimidazolidin-4-yl]urea · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.53 | 0.85 | 25 | 3AL |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 2Q37 · Crystal structure of OHCU decarboxylase in the presence of (S)-allantoin · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LVM5 · AlphaFold monomer V2.0 prediction for uric acid degradation bifunctional protein ttl… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9LVM5
- Elsewhere: RCSB PDB 2Q37 · PDBe 2Q37 · UniProt Q9LVM5
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