Research workbench
Anti-marburgvirus nucleoprotein single domain antibody C complexed with nucleoprotein C-terminal domain
Analyse Anti-marburgvirus nucleoprotein single domain antibody C complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W2Q
- Type
- protein
- Length
- 727 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-marburgvirus nucleoprotein single domain antibody C; Nucleoprotein
- UniProt
- P27588
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 5 distinct chains · 29% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Anti-marburgvirus nucleoprotein single domain antibody C | protein | 116 | 8% helix, 52% strand | — |
| B | Nucleoprotein | protein | 67 | 54% helix, 12% strand | P27588 |
| C, G | Anti-marburgvirus nucleoprotein single domain antibody C | protein | 117 | 8% helix, 52% strand | — |
| D, H | Nucleoprotein | protein | 63 | 57% helix, 13% strand | P27588 |
| F | Nucleoprotein | protein | 68 | 53% helix, 12% strand | P27588 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 881 | 0.78 | 0.81 | 71 | empty |
| 2 | 765 | 0.76 | 0.81 | 79 | empty |
| 3 | 390 | 0.59 | 0.76 | 43 | empty |
| 4 | 100 | 0.46 | 0.80 | 25 | empty |
| 5 | 60 | 0.43 | 0.83 | 18 | empty |
Interfaces
16 interfaces between chains.
- E–F · 714 Ų buried · 10 hydrogen bonds · protein-protein
- G–H · 704 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 703 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 694 Ų buried · 7 hydrogen bonds · protein-protein
- E–G · 435 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4W2Q · Anti-Marburgvirus Nucleoprotein Single Domain Antibody C Complexed with Nucleoprotein… · 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
- Every structure of UniProt P27588
- Elsewhere: RCSB PDB 4W2Q · PDBe 4W2Q · UniProt P27588
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