Research workbench
Solution structure of the rmm-ctd domains of human line-1 ORF1P
Analyse Solution structure of the rmm-ctd domains of human line-1 ORF1P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LDY
- Type
- protein
- Length
- 176 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ORF1 codes for a 40 kda product
- UniProt
- Q15605
- Pockets
- 2 · best druggability 0.29
Structure
solution nmr · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ORF1 codes for a 40 kda product | protein | 176 | 41% helix, 22% strand | Q15605 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.29 | 0.75 | 13 | empty |
| 2 | 62 | 0.27 | 0.73 | 10 | empty |
Compared structures
- 2LDY · Solution structure of the RMM-CTD domains of human LINE-1 ORF1p · 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 Q15605
- Elsewhere: RCSB PDB 2LDY · PDBe 2LDY · UniProt Q15605
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