MolNFT v1 · #156136 · protein
Crystal structure of N(OMEGA)-hydroxy-L-arginine hydrolase
6LUG: “Crystal structure of N(OMEGA)-hydroxy-L-arginine hydrolase”. X-ray diffraction, 1 ligand (MN). MolNFT v1 #156136 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6LUG
- Type
- protein
- Length
- 544 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D2Z025
- Ligands
- MN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 271 | — | D2Z025 |
| B | — | protein | 273 | — | D2Z025 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LUG · Crystal 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 6LUG · PDBe 6LUG · UniProt D2Z025
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