MolNFT v1 · #20585 · protein
Crystal structure of the camelid single domain antibody cab-LYS2 in complex with hen egg white lysozyme
1RJC · Camelid heavy chain antibody: “Crystal structure of the camelid single domain antibody cab-LYS2 in complex with hen egg white lysozyme”. X-ray diffraction, 1 ligand (PO4), 2 pockets (best druggability 0.59). MolNFT v1 #20585 on…
- PDB
- 1RJC
- Type
- protein
- Length
- 252 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camelid heavy chain antibody; Lysozyme C
- EC
- 3.2.1.17
- UniProt
- P00698
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camelid heavy chain antibody | protein | 123 | 5% helix, 44% strand | — |
| B | Lysozyme C (EC 3.2.1.17) | protein | 129 | 40% helix, 11% strand | P00698 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.59 | 0.81 | 26 | empty |
| 2 | 186 | 0.47 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 841 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1RJC · Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg… · 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 1RJC · PDBe 1RJC · UniProt P00698
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