Research workbench
Dithiol alpha melanotropin peptide cyclized via rhenium metal coordination
Analyse Dithiol alpha melanotropin peptide cyclized via rhenium metal coordination in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B0Q
- Type
- protein
- Length
- 10 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (cyclic alpha melanocyte stimulating hormone)
- Ligands
- ACE, RE, NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (cyclic alpha melanocyte stimulating hormone) | protein | 10 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- RE · Rhenium · metal · chains A
- NH2 · Amino group · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent, 1 d-amino (covalent ligand, D-amino acid).
Compared structures
- 1B0Q · Dithiol alpha melanotropin peptide cyclized via rhenium metal coordination · 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
- Elsewhere: RCSB PDB 1B0Q · PDBe 1B0Q
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