Research workbench
Rrm domain from C. elegans sup-12
Analyse Rrm domain from C. elegans sup-12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CH0
- Type
- protein
- Length
- 97 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein sup-12, isoform B
- UniProt
- H2L051
Structure
solution nmr · 1 distinct chain · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| S | Protein sup-12, isoform B | protein | 97 | 24% helix, 31% strand | H2L051 |
Compared structures
- 4CH0 · RRM domain from C. elegans SUP-12 · the same entry in another collection · chain S against S, 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 4CH0 · PDBe 4CH0 · UniProt H2L051
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