Research workbench
NMR structure of guanylyl cyclase activator protein 1 (GCAP1) mutant V77E in a CA2+-FREE/MG2+-bound activator state
Analyse NMR structure of guanylyl cyclase activator protein 1 (GCAP1) mutant V77E in a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NA0
- Type
- protein
- Length
- 184 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanylyl cyclase-activating protein 1
- UniProt
- P46065
- Ligands
- MYR
- Pockets
- 5 · best druggability 0.76
Structure
solution nmr · 1 distinct chain · 61% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanylyl cyclase-activating protein 1 | protein | 184 | 61% helix, 4% strand | P46065 |
Ligands and binding sites
- MYR · Myristic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 365 | 0.76 | 0.86 | 44 | MYR |
| 2 | 148 | 0.72 | 0.91 | 35 | empty |
| 3 | 78 | 0.53 | 0.85 | 18 | empty |
| 4 | 113 | 0.43 | 0.76 | 19 | empty |
| 5 | 60 | 0.33 | 0.77 | 14 | empty |
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 2NA0 · NMR structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) mutant V77E in a… · the same entry in another collection · chain A against A, TM-score 1.00
- P46065 · AlphaFold monomer V2.0 prediction for guanylyl cyclase-activating protein 1 (P46065) · a predicted model of the same protein · chain A against A, TM-score 0.61
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 P46065
- Elsewhere: RCSB PDB 2NA0 · PDBe 2NA0 · UniProt P46065
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