Research workbench
Fab 3B6 bound to APOL1 ntd
Analyse Fab 3B6 bound to APOL1 ntd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LFA
- Type
- protein
- Length
- 1,058 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apolipoprotein L1; Fab 3B6 heavy chain; Fab 3B6 light chain
- UniProt
- O14791
- Ligands
- CL
- Pockets
- 11 · best druggability 0.69
Structure
x-ray diffraction · 4 distinct chains · 31% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apolipoprotein L1 | protein | 94 | 82% helix, 0% strand | O14791 |
| B, H | Fab 3B6 heavy chain | protein | 220 | 10% helix, 51% strand | — |
| C | Apolipoprotein L1 | protein | 100 | 81% helix, 0% strand | O14791 |
| D, L | Fab 3B6 light chain | protein | 212 | 8% helix, 52% strand | — |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains B, D, L
- GOL · Glycerol · additive · 2 copies · chains B, H, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 993 | 0.69 | 0.74 | 108 | GOL |
| 2 | 545 | 0.59 | 0.73 | 59 | empty |
| 3 | 149 | 0.45 | 0.76 | 35 | CL |
| 4 | 124 | 0.44 | 0.76 | 19 | empty |
| 5 | 102 | 0.43 | 0.78 | 27 | empty |
Interfaces
7 interfaces between chains.
- H–L · 1832 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 1769 Ų buried · 12 hydrogen bonds · protein-protein
- C–H · 378 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 362 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 361 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
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 O14791
- Elsewhere: RCSB PDB 7LFA · PDBe 7LFA · UniProt O14791
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