Research workbench
The structure of the camelid antibody CABHUL5 in complex with human lysozyme
Analyse The structure of the camelid antibody CABHUL5 in complex with human lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I0C
- Type
- protein
- Length
- 513 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme C; CABHUL5 antibody
- EC
- 3.2.1.17
- UniProt
- P61626
- Ligands
- CL
- Pockets
- 3 · best druggability 0.31
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lysozyme C (EC 3.2.1.17) | protein | 130 | 38% helix, 12% strand | P61626 |
| C | CABHUL5 antibody | protein | 126 | 7% helix, 49% strand | — |
| D | CABHUL5 antibody | protein | 127 | 9% helix, 50% strand | — |
Ligands and binding sites
- CL · Chloride ion · ion · 7 copies · chains A, D, B, C
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 70 | 0.31 | 0.74 | 17 | empty |
| 2 | 56 | 0.30 | 0.76 | 14 | GOL |
| 3 | 57 | 0.28 | 0.73 | 13 | empty |
Interfaces
2 interfaces between chains.
- B–C · 705 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 683 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 4I0C · The structure of the camelid antibody cAbHuL5 in complex with 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 4I0C · PDBe 4I0C · UniProt P61626
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