Research workbench
A picomolar affinity FN3 domain in complex with hen egg-white lysozyme
Analyse A picomolar affinity FN3 domain in complex with hen egg-white lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5J7C
- Type
- protein
- Length
- 452 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme C; FNFN10-anti-lysozyme (DE0.4.1)
- EC
- 3.2.1.17
- UniProt
- P00698
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 4 distinct chains · 23% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme C (EC 3.2.1.17) | protein | 129 | 41% helix, 12% strand | P00698 |
| B | Lysozyme C (EC 3.2.1.17) | protein | 128 | 41% helix, 12% strand | P00698 |
| C | FNFN10-anti-lysozyme (DE0.4.1) | protein | 97 | 0% helix, 51% strand | — |
| D | FNFN10-anti-lysozyme (DE0.4.1) | protein | 98 | 0% helix, 49% strand | — |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.63 | 0.77 | 46 | empty |
Interfaces
5 interfaces between chains.
- A–C · 927 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 923 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 352 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 184 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 181 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 5J7C · A picomolar affinity FN3 domain in complex with hen egg-white 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 5J7C · PDBe 5J7C · UniProt P00698
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