MolNFT v1 · #17467 · protein
Contribution of hydrophobic residues to the stability of human lysozyme: X-ray structure of the V93A mutant
1OUI: “Contribution of hydrophobic residues to the stability of human lysozyme: X-ray structure of the V93A mutant”. X-ray diffraction, 1 ligand (NA), 1 pocket (best druggability 0.32). MolNFT v1 #17467 on GenesisL1: 3D structure, binding…
- PDB
- 1OUI
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme
- EC
- 3.2.1.17
- UniProt
- P61626
- Ligands
- NA
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme (EC 3.2.1.17) | protein | 130 | 38% helix, 12% strand | P61626 |
Ligands and binding sites
- NA · Sodium ion · metal
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.32 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1OUI · Contribution of hydrophobic residues to the stability of human lysozyme: X-ray structure… · the same entry in another collection · 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 P61626
- Elsewhere: RCSB PDB 1OUI · PDBe 1OUI · UniProt P61626
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