MolNFT v2 · #1578 · protein
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six ser->ala mutants
1B5Y · Protein (lysozyme): “Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray…”. X-ray diffraction at 2.2, 1 ligand (NA), 1 pocket (best druggability 0.33). MolNFT v2 #1578 on…
- PDB
- 1B5Y
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Homo sapiens
- Molecule
- Protein (lysozyme)
- EC
- 3.2.1.17
- UniProt
- P61626
- Ligands
- NA
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · resolution 2.2 · 1 distinct chain · 38% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (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 | 64 | 0.33 | 0.76 | 12 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1B5Y · Contribution of hydrogen bonds to the conformational stability of human lysozyme… · the same entry in another collection · chain A against A, TM-score 1.00
- P61626 · AlphaFold monomer V2.0 prediction for lysozyme C (P61626) · a predicted model of the same protein · chain A 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 P61626
- Elsewhere: RCSB PDB 1B5Y · PDBe 1B5Y · UniProt P61626
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