Research workbench
Crystal structure of alpha-momorcharin in complex with camp
Analyse Crystal structure of alpha-momorcharin in complex with camp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LOQ
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16094
- Ligands
- CMP
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 246 | — | P16094 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LOQ · crystal structure of alpha-momorcharin in complex with cAMP · the same entry in another collection · chain A against A, TM-score 1.00
- P16094 · AlphaFold monomer V2.0 prediction for ribosome-inactivating protein momordin I (P16094) · a predicted model of the same protein · 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
- Every structure of UniProt P16094
- Elsewhere: RCSB PDB 6LOQ · PDBe 6LOQ · UniProt P16094
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