Research workbench
Anti-sudan ebolavirus nucleoprotein single domain antibody sudan B (sb) complexed with sudan ebolavirus nucleoprotein C-terminal domain 610-738
Analyse Anti-sudan ebolavirus nucleoprotein single domain antibody sudan B (sb)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U51
- Type
- protein
- Length
- 418 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-sudan ebolavirus nucleoprotein single domain antibody sudan B (sb); Nucleoprotein
- UniProt
- Q9QP77
- Pockets
- 7 · best druggability 0.53
Structure
x-ray diffraction · 4 distinct chains · 24% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Anti-sudan ebolavirus nucleoprotein single domain antibody sudan B (sb) | protein | 118 | 3% helix, 53% strand | — |
| B | Nucleoprotein | protein | 92 | 50% helix, 15% strand | Q9QP77 |
| A | Anti-sudan ebolavirus nucleoprotein single domain antibody sudan B (sb) | protein | 119 | 3% helix, 52% strand | — |
| D | Nucleoprotein | protein | 89 | 55% helix, 9% strand | Q9QP77 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.53 | 0.79 | 23 | empty |
| 2 | 103 | 0.46 | 0.79 | 22 | empty |
| 3 | 116 | 0.43 | 0.77 | 26 | empty |
| 4 | 82 | 0.36 | 0.76 | 16 | empty |
| 5 | 82 | 0.35 | 0.75 | 15 | empty |
Interfaces
6 interfaces between chains.
- C–D · 776 Ų buried · 11 hydrogen bonds · protein-protein
- B–A · 726 Ų buried · 10 hydrogen bonds · protein-protein
- C–B · 703 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 690 Ų buried · 9 hydrogen bonds · protein-protein
- C–A · 111 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6U51 · Anti-Sudan ebolavirus Nucleoprotein Single Domain Antibody Sudan B (SB) Complexed with… · the same entry in another collection · chain C against C, 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 Q9QP77
- Elsewhere: RCSB PDB 6U51 · PDBe 6U51 · UniProt Q9QP77
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