MolNFT v1 · #1578 · protein
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six ser->ala mutants
1B5Z: “Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray…”. X-ray diffraction, 3 pockets (best druggability 0.46). MolNFT v1 #1578 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1B5Z
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme
- EC
- 3.2.1.17
- UniProt
- P61626
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lysozyme (EC 3.2.1.17) | protein | 130 | 38% helix, 12% strand | P61626 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.46 | 0.76 | 23 | empty |
| 2 | 105 | 0.37 | 0.74 | 20 | empty |
| 3 | 68 | 0.34 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 515 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1B5Z · 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
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 1B5Z · PDBe 1B5Z · UniProt P61626
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