Research workbench
Context-independent anti-hypusine antibody FABHPU24.B in complex with hypusine
Analyse Context-independent anti-hypusine antibody FABHPU24.B in complex with hypusine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DSC
- Type
- protein
- Length
- 1,710 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab HPU24.B heavy chain; Fab HOU24.B light chain; Peptide: gly-hpu-gly-ser-gly
- Pockets
- 13 · best druggability 0.66
Structure
x-ray diffraction · 8 distinct chains · 7% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fab HPU24.B heavy chain | protein | 212 | 6% helix, 57% strand | — |
| B, D | Fab HOU24.B light chain | protein | 212 | 8% helix, 52% strand | — |
| C | Fab HPU24.B heavy chain | protein | 210 | 6% helix, 56% strand | — |
| E | Fab HPU24.B heavy chain | protein | 213 | 6% helix, 57% strand | — |
| F | Fab HOU24.B light chain | protein | 211 | 8% helix, 51% strand | — |
| H | Fab HPU24.B heavy chain | protein | 211 | 6% helix, 56% strand | — |
| L | Fab HOU24.B light chain | protein | 209 | 9% helix, 51% strand | — |
| P, Q, M, N | Peptide: gly-hpu-gly-ser-gly | protein | 5 | 0% helix, 0% strand | — |
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 750 | 0.66 | 0.75 | 85 | empty |
| 2 | 410 | 0.62 | 0.77 | 52 | empty |
| 3 | 617 | 0.62 | 0.74 | 63 | empty |
| 4 | 404 | 0.61 | 0.77 | 50 | empty |
| 5 | 476 | 0.59 | 0.74 | 60 | empty |
Interfaces
18 interfaces between chains.
- E–F · 1887 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1880 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1870 Ų buried · 15 hydrogen bonds · protein-protein
- H–L · 1818 Ų buried · 18 hydrogen bonds · protein-protein
- D–L · 366 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 23 disulfide, 6 modified (disulfide, nonstandard, cyclization).
Compared structures
- 5DSC · Context-independent anti-hypusine antibody FabHpu24.B in complex with hypusine · 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 5DSC · PDBe 5DSC
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