Research workbench
NMR structure of the ECD1 of crf-R1 in complex with a peptide agonist
Analyse NMR structure of the ECD1 of crf-R1 in complex with a peptide agonist in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L27
- Type
- protein
- Length
- 122 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Corticotropin-releasing factor receptor 1; Peptide agonist
- UniProt
- P34998
Structure
solution nmr · 2 distinct chains · 32% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Corticotropin-releasing factor receptor 1 | protein | 84 | 12% helix, 13% strand | P34998 |
| B | Peptide agonist | protein | 38 | 76% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 645 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2L27 · NMR Structure of the ECD1 of CRF-R1 in complex with a peptide agonist · the same entry in another collection · chain B against B, TM-score 1.00
- P34998 · AlphaFold monomer V2.0 prediction for corticotropin-releasing factor receptor 1 (P34998) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 P34998
- Elsewhere: RCSB PDB 2L27 · PDBe 2L27 · UniProt P34998
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.