Research workbench
Crystal structure of C-terminal domain of PABPC1 in complex with nucleoprotein from human coronavirus 229E
Analyse Crystal structure of C-terminal domain of PABPC1 in complex with nucleoprotein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BN3
- Type
- protein
- Length
- 286 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2 of polyadenylate-binding protein 1; Nucleoprotein from human coronavirus 229E
- UniProt
- P11940
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 3 distinct chains · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Isoform 2 of polyadenylate-binding protein 1 | protein | 83 | 82% helix, 0% strand | P11940 |
| F, D | Nucleoprotein from human coronavirus 229E | protein | 12 | 0% helix, 0% strand | — |
| E | Nucleoprotein from human coronavirus 229E | protein | 13 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.33 | 0.74 | 15 | empty |
Interfaces
8 interfaces between chains.
- A–B · 688 Ų buried · 7 hydrogen bonds · protein-protein
- B–E · 672 Ų buried · 6 hydrogen bonds · protein-protein
- C–F · 663 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 657 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 114 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7BN3 · Crystal structure of C-terminal domain of PABPC1 in complex with Nucleoprotein from Human… · 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 P11940
- Elsewhere: RCSB PDB 7BN3 · PDBe 7BN3 · UniProt P11940
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