Research workbench
High resolution structure of N(OMEGA)-hydroxy-L-arginine hydrolase
Analyse High resolution structure of N(OMEGA)-hydroxy-L-arginine hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LUH
- Type
- protein
- Length
- 544 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N(OMEGA)-hydroxy-L-arginine amidinohydrolase
- EC
- 3.5.3.25
- UniProt
- D2Z025
- Ligands
- MN, MG
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N(OMEGA)-hydroxy-L-arginine amidinohydrolase (EC 3.5.3.25) | protein | 271 | 45% helix, 15% strand | D2Z025 |
| B | N(OMEGA)-hydroxy-L-arginine amidinohydrolase (EC 3.5.3.25) | protein | 273 | 46% helix, 15% strand | D2Z025 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 542 | 0.77 | 0.84 | 50 | empty |
| 2 | 202 | 0.66 | 0.85 | 33 | empty |
| 3 | 104 | 0.48 | 0.81 | 21 | empty |
| 4 | 61 | 0.30 | 0.75 | 23 | MG |
Interfaces
1 interface between chains.
- A–B · 1236 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 6LUH · High resolution structure of N(omega)-hydroxy-L-arginine hydrolase · the same entry in another collection · chain A against A, TM-score 1.00
- D2Z025 · AlphaFold monomer V2.0 prediction for N(OMEGA)-hydroxy-L-arginine amidinohydrolase… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 D2Z025
- Elsewhere: RCSB PDB 6LUH · PDBe 6LUH · UniProt D2Z025
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