Research workbench
Crystal structure of G alpha 12 in complex with GDP, MG2+ and ALF4-
Analyse Crystal structure of G alpha 12 in complex with GDP, MG2+ and ALF4- in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZCA
- Type
- protein
- Length
- 635 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- G alpha I/12
- UniProt
- P27600
- Ligands
- ALF, GDP, MG
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | G alpha I/12 | protein | 318 | 50% helix, 13% strand | P27600 |
| B | G alpha I/12 | protein | 317 | 50% helix, 13% strand | P27600 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · 2 copies · chains A, B
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 724 | 0.82 | 0.86 | 96 | MG, ALF, GDP |
| 2 | 341 | 0.76 | 0.87 | 57 | MG, ALF, GDP |
| 3 | 149 | 0.59 | 0.83 | 18 | empty |
| 4 | 108 | 0.54 | 0.83 | 17 | empty |
| 5 | 191 | 0.53 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 522 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1ZCA · Crystal structure of G alpha 12 in complex with GDP, Mg2+ and AlF4- · the same entry in another collection · chain A against A, TM-score 1.00
- P27600 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein subunit alpha-12… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P27600
- Elsewhere: RCSB PDB 1ZCA · PDBe 1ZCA · UniProt P27600
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