Research workbench
Anti-lewis X Fab fragment uncomplexed
Analyse Anti-lewis X Fab fragment uncomplexed in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UZ6
- Type
- protein
- Length
- 1,684 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IgG Fab (IGG3, kappa) light chain 291-2G3-a; IgG Fab (IGG3, kappa) heavy chain 291-2G3-a
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.67
Structure
x-ray diffraction · 7 distinct chains · 7% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, L | IgG Fab (IGG3, kappa) light chain 291-2G3-a | protein | 210 | 6% helix, 49% strand | — |
| F | IgG Fab (IGG3, kappa) heavy chain 291-2G3-a | protein | 208 | 9% helix, 51% strand | — |
| H | IgG Fab (IGG3, kappa) heavy chain 291-2G3-a | protein | 210 | 9% helix, 52% strand | — |
| M | IgG Fab (IGG3, kappa) light chain 291-2G3-a | protein | 211 | 6% helix, 53% strand | — |
| P | IgG Fab (IGG3, kappa) heavy chain 291-2G3-a | protein | 211 | 7% helix, 52% strand | — |
| V | IgG Fab (IGG3, kappa) light chain 291-2G3-a | protein | 212 | 7% helix, 50% strand | — |
| W | IgG Fab (IGG3, kappa) heavy chain 291-2G3-a | protein | 212 | 7% helix, 52% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains E, L, M, V
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 433 | 0.67 | 0.79 | 72 | empty |
| 2 | 447 | 0.64 | 0.77 | 42 | empty |
| 3 | 312 | 0.63 | 0.80 | 46 | empty |
| 4 | 330 | 0.63 | 0.79 | 47 | empty |
| 5 | 257 | 0.60 | 0.80 | 42 | empty |
Interfaces
16 interfaces between chains.
- V–W · 1705 Ų buried · 18 hydrogen bonds · protein-protein
- H–L · 1667 Ų buried · 20 hydrogen bonds · protein-protein
- E–F · 1655 Ų buried · 19 hydrogen bonds · protein-protein
- M–P · 1644 Ų buried · 15 hydrogen bonds · protein-protein
- M–V · 234 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 1UZ6 · anti-Lewis X Fab fragment uncomplexed · the same entry in another collection · chain E against E, 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 1UZ6 · PDBe 1UZ6
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