MolNFT v1 · #12826 · protein + DNA
Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex
1KSX · E1 recognition sequence: “Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex”. X-ray diffraction, 20 pockets (best druggability 0.72). MolNFT v1 #12826 on GenesisL1: 3D…
- PDB
- 1KSX
- Type
- protein + DNA
- Length
- 1,244 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E1 recognition sequence; Replication protein E1
- UniProt
- P03116
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, G, K, O | E1 recognition sequence | dna | 21 | — | — |
| A, B, E, F, I, J, M, N | Replication protein E1 | protein | 145 | 40% helix, 30% strand | P03116 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 543 | 0.72 | 0.81 | 52 | empty |
| 2 | 455 | 0.72 | 0.82 | 46 | empty |
| 3 | 1053 | 0.70 | 0.75 | 61 | empty |
| 4 | 455 | 0.70 | 0.81 | 40 | empty |
| 5 | 416 | 0.67 | 0.80 | 38 | empty |
Interfaces
34 interfaces between chains.
- C–G · 797 Ų buried · 58 hydrogen bonds · nucleic-nucleic
- K–O · 795 Ų buried · 68 hydrogen bonds · nucleic-nucleic
- I–N · 453 Ų buried · 0 hydrogen bonds · protein-protein
- B–E · 445 Ų buried · 2 hydrogen bonds · protein-protein
- A–F · 439 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1KSX · Crystal Structures of Two Intermediates in the Assembly of the Papillomavirus Replication… · 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 P03116
- Elsewhere: RCSB PDB 1KSX · PDBe 1KSX · UniProt P03116
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