Research workbench
Structure for antibody hyhel-63 Y33I mutant complexed with hen egg lysozyme
Analyse Structure for antibody hyhel-63 Y33I mutant complexed with hen egg lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XGR
- Type
- protein
- Length
- 554 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antibody kappa light chain; Antibody kappa heavy chain; Lysozyme C
- EC
- 3.2.1.17
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 3 distinct chains · 14% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antibody kappa light chain | protein | 215 | 6% helix, 53% strand | — |
| B | Antibody kappa heavy chain | protein | 210 | 7% helix, 52% strand | — |
| C | Lysozyme C (EC 3.2.1.17) | protein | 129 | 40% helix, 11% strand | — |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.65 | 0.82 | 38 | empty |
| 2 | 364 | 0.55 | 0.74 | 52 | empty |
| 3 | 193 | 0.50 | 0.76 | 27 | empty |
| 4 | 84 | 0.34 | 0.74 | 17 | empty |
| 5 | 79 | 0.31 | 0.73 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1846 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 535 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 421 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 1XGR · Structure for antibody HyHEL-63 Y33I mutant complexed with hen egg 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
- Elsewhere: RCSB PDB 1XGR · PDBe 1XGR
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