Research workbench
Focus refinement of soluble domain of adenylyl cyclase 9 in complex with darpin C4 and mant-GTP
Analyse Focus refinement of soluble domain of adenylyl cyclase 9 in complex with darpin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PDD
- Type
- protein
- Length
- 577 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E1BM79
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 449 | — | E1BM79 |
| B | — | protein | 128 | — | — |
Compared structures
- 7PDD · Focus refinement of soluble domain of Adenylyl cyclase 9 in complex with DARPin C4 and… · 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
- Every structure of UniProt E1BM79
- Elsewhere: RCSB PDB 7PDD · PDBe 7PDD · UniProt E1BM79
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