Research workbench
Crystal structure of hyhel-10 fv-hen lysozyme complex
Analyse Crystal structure of hyhel-10 fv-hen lysozyme complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C08
- Type
- protein
- Length
- 350 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-hen egg white lysozyme antibody (hyhel-10); Lysozyme
- UniProt
- P01642, P01823, P00698
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-hen egg white lysozyme antibody (hyhel-10) | protein | 107 | 3% helix, 50% strand | P01642 |
| B | Anti-hen egg white lysozyme antibody (hyhel-10) | protein | 114 | 8% helix, 51% strand | P01823 |
| C | Lysozyme | protein | 129 | 40% helix, 11% strand | P00698 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.64 | 0.88 | 28 | empty |
| 2 | 77 | 0.34 | 0.75 | 13 | empty |
| 3 | 62 | 0.27 | 0.73 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 776 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 595 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 417 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1C08 · Crystal structure of hyhel-10 fv-hen lysozyme complex · the same entry in another collection · chain A against A, TM-score 1.00
- P01823 · AlphaFold monomer V2.0 prediction for ig heavy chain V region 36-60 (P01823) · a predicted model of the same protein · chain B against A, TM-score 0.96
- P01642 · AlphaFold monomer V2.0 prediction for ig kappa chain V-V region L7 (P01642) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P01642
- Every structure of UniProt P01823
- Every structure of UniProt P00698
- Elsewhere: RCSB PDB 1C08 · PDBe 1C08 · UniProt P01642 · UniProt P01823 · UniProt P00698
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