Research workbench
The solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor (rlf)
Analyse The solution structure of a conformationally restricted fully active derivative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K6U
- Type
- protein
- Length
- 54 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin-like 3 a chain; Insulin-like 3 B chain
- UniProt
- P51460
Structure
solution nmr · 2 distinct chains · 41% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin-like 3 a chain | protein | 27 | 44% helix, 4% strand | P51460 |
| B | Insulin-like 3 B chain | protein | 27 | 37% helix, 4% strand | P51460 |
Interfaces
1 interface between chains.
- A–B · 685 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 1 isopeptide (disulfide, isopeptide).
Compared structures
- 2K6U · The Solution Structure of a Conformationally Restricted Fully Active Derivative of the… · the same entry in another collection · chain A against A, TM-score 1.00
- P51460 · AlphaFold monomer V2.0 prediction for insulin-like 3 (P51460) · a predicted model of the same protein · chain A against A, TM-score 0.59
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 P51460
- Elsewhere: RCSB PDB 2K6U · PDBe 2K6U · UniProt P51460
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.