Research workbench
Adeno-associated virus 2 REP68 hd-heptamer-ssdna with atpgs
Analyse Adeno-associated virus 2 REP68 hd-heptamer-ssdna with atpgs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JSG
- Type
- protein + DNA
- Length
- 1,921 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein REP68; DNA (5'- D(P*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3')
- EC
- 3.6.4.12
- UniProt
- P03132
- Pockets
- 16 · best druggability 0.69
Structure
electron microscopy · 2 distinct chains · 40% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Protein REP68 (EC 3.6.4.12) | protein | 272 | 40% helix, 11% strand | P03132 |
| N | DNA (5'- D(P*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3') | dna | 17 | — | — |
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 833 | 0.69 | 0.76 | 81 | empty |
| 2 | 796 | 0.68 | 0.76 | 73 | empty |
| 3 | 804 | 0.68 | 0.76 | 78 | empty |
| 4 | 769 | 0.67 | 0.76 | 78 | empty |
| 5 | 752 | 0.66 | 0.75 | 77 | empty |
Interfaces
9 interfaces between chains.
- F–G · 123 Ų buried · 0 hydrogen bonds · protein-protein
- D–E · 101 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 83 Ų buried · 1 hydrogen bond · protein-protein
- E–F · 79 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 59 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7JSG · Adeno-Associated Virus 2 Rep68 HD-Heptamer-ssDNA with ATPgS · 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 P03132
- Elsewhere: RCSB PDB 7JSG · PDBe 7JSG · UniProt P03132
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