Research workbench
Humanized anti-lysozyme fv complexed with lysozyme
Analyse Humanized anti-lysozyme fv complexed with lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BVK
- Type
- protein
- Length
- 706 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HULYS11; Lysozyme
- EC
- 3.2.1.17
- UniProt
- P00698
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | HULYS11 | protein | 108 | 3% helix, 48% strand | — |
| B, E | HULYS11 | protein | 116 | 3% helix, 52% strand | — |
| C, F | Lysozyme (EC 3.2.1.17) | protein | 129 | 36% helix, 11% strand | P00698 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.70 | 0.95 | 23 | empty |
| 2 | 85 | 0.68 | 0.93 | 22 | empty |
| 3 | 64 | 0.32 | 0.75 | 15 | empty |
| 4 | 66 | 0.30 | 0.74 | 17 | empty |
| 5 | 55 | 0.30 | 0.75 | 12 | empty |
Interfaces
6 interfaces between chains.
- D–E · 788 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 787 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 440 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 415 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 392 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 1BVK · Humanized anti-lysozyme fv complexed with 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 P00698
- Elsewhere: RCSB PDB 1BVK · PDBe 1BVK · UniProt P00698
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.