Research workbench
Crystal structure of aquifex aeolicus era Y63A bound to GDP.ALF4-
Analyse Crystal structure of aquifex aeolicus era Y63A bound to GDP.ALF4- in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C1O
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase era
- UniProt
- O67800
- Ligands
- ALF, GDP, MG, K
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase era | protein | 301 | 40% helix, 23% strand | O67800 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- K · Potassium ion · metal · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.55 | 0.85 | 36 | empty |
| 2 | 110 | 0.54 | 0.83 | 27 | ALF, GDP, MG, K |
| 3 | 111 | 0.41 | 0.76 | 17 | empty |
Compared structures
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 O67800
- Elsewhere: RCSB PDB 7C1O · PDBe 7C1O · UniProt O67800
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