Research workbench
Crystal structure of FAB4201 raised against human erythrocyte anion exchanger 1
Analyse Crystal structure of FAB4201 raised against human erythrocyte anion exchanger 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A16
- Type
- protein
- Length
- 1,776 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAB4201 heavy chain
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | FAB4201 heavy chain | protein | 226 | 4% helix, 51% strand | — |
| B, D, F, H | FAB4201 heavy chain | protein | 218 | 6% helix, 54% strand | — |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 960 | 0.78 | 0.81 | 89 | empty |
| 2 | 424 | 0.67 | 0.80 | 54 | empty |
| 3 | 274 | 0.64 | 0.81 | 37 | empty |
| 4 | 595 | 0.62 | 0.74 | 51 | empty |
| 5 | 528 | 0.61 | 0.75 | 50 | empty |
Interfaces
11 interfaces between chains.
- E–F · 2222 Ų buried · 25 hydrogen bonds · protein-protein
- G–H · 2191 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 2173 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 2162 Ų buried · 23 hydrogen bonds · protein-protein
- C–H · 313 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 5A16 · Crystal structure of Fab4201 raised against Human Erythrocyte Anion Exchanger 1 · 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 5A16 · PDBe 5A16
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