Research workbench
Complex HCV core-Fab 19D9D6-protein L mutant (D55A,L57H,Y64W) in space group P21
Analyse Complex HCV core-Fab 19D9D6-protein L mutant (D55A,L57H,Y64W) in space group P21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XCQ
- Type
- protein
- Length
- 2,117 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein C; Monoclonal antibody 19D9D6 light chain; Monoclonal antibody 19D9D6…
- UniProt
- P26661
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 8 distinct chains · 9% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Capsid protein C | protein | 24 | 0% helix, 0% strand | P26661 |
| A, C, E | Monoclonal antibody 19D9D6 light chain | protein | 220 | 7% helix, 34% strand | — |
| B, D, F, H | Monoclonal antibody 19D9D6 heavy chain | protein | 218 | 4% helix, 33% strand | — |
| L | Protein L | protein | 66 | 24% helix, 26% strand | — |
| Q, S | Capsid protein C | protein | 44 | 0% helix, 0% strand | P26661 |
| M, O | Protein L | protein | 62 | 29% helix, 23% strand | — |
| N | Protein L | protein | 64 | 17% helix, 28% strand | — |
| G | Monoclonal antibody 19D9D6 light chain | protein | 219 | 5% helix, 34% strand | — |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 591 | 0.78 | 0.84 | 68 | empty |
| 2 | 587 | 0.71 | 0.80 | 57 | empty |
| 3 | 668 | 0.69 | 0.77 | 63 | empty |
| 4 | 263 | 0.60 | 0.79 | 31 | empty |
| 5 | 240 | 0.60 | 0.80 | 30 | empty |
Interfaces
20 interfaces between chains.
- E–F · 1838 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1776 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1770 Ų buried · 16 hydrogen bonds · protein-protein
- G–H · 1761 Ų buried · 12 hydrogen bonds · protein-protein
- C–M · 722 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 1XCQ · Complex HCV core-Fab 19D9D6-Protein L mutant (D55A,L57H,Y64W) in space group P21 · the same entry in another collection · chain P against P, 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 P26661
- Elsewhere: RCSB PDB 1XCQ · PDBe 1XCQ · UniProt P26661
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