Research workbench
NMR structure of GCAP5
Analyse NMR structure of GCAP5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M2M
- Type
- protein
- Length
- 182 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanylate cyclase activator 1A
- UniProt
- Q5MAC8
- Ligands
- MYR, MG
- Pockets
- 1 · best druggability 0.85
Structure
solution nmr · 1 distinct chain · 57% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanylate cyclase activator 1A | protein | 182 | 57% helix, 3% strand | Q5MAC8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 869 | 0.85 | 0.87 | 90 | MYR |
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 7M2M · NMR Structure of GCAP5 · 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 Q5MAC8
- Elsewhere: RCSB PDB 7M2M · PDBe 7M2M · UniProt Q5MAC8
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