Research workbench
Rrm domain from C. elegans sup-12 bound to ggtgtgc DNA
Analyse Rrm domain from C. elegans sup-12 bound to ggtgtgc DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CH1
- Type
- protein + DNA
- Length
- 104 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein sup-12, isoform B; Ggtgtgc
- UniProt
- H2L051
- Pockets
- 2 · best druggability 0.50
Structure
solution nmr · 2 distinct chains · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein sup-12, isoform B | protein | 97 | 24% helix, 31% strand | H2L051 |
| B | Ggtgtgc | dna | 7 | — | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.50 | 0.81 | 19 | empty |
| 2 | 80 | 0.40 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 854 Ų buried · 19 hydrogen bonds · protein-nucleic
Compared structures
- 4CH1 · RRM domain from C. elegans SUP-12 bound to GGTGTGC DNA · the same entry in another collection · chain B against B, 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 H2L051
- Elsewhere: RCSB PDB 4CH1 · PDBe 4CH1 · UniProt H2L051
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