Research workbench
Crystal structure of mouse amf / A5P complex
Analyse Crystal structure of mouse amf / A5P complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CXP
- Type
- protein
- Length
- 1,114 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-6-phosphate isomerase
- EC
- 5.3.1.9
- UniProt
- P06745
- Ligands
- A5P
- Pockets
- 14 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 557 | 53% helix, 13% strand | P06745 |
Ligands and binding sites
- A5P · Arabinose-5-phosphate · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1027 | 0.77 | 0.79 | 65 | empty |
| 2 | 342 | 0.70 | 0.83 | 48 | A5P |
| 3 | 157 | 0.69 | 0.89 | 35 | A5P |
| 4 | 126 | 0.51 | 0.80 | 15 | empty |
| 5 | 61 | 0.43 | 0.82 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 6661 Ų buried · 92 hydrogen bonds · protein-protein
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 P06745
- Elsewhere: RCSB PDB 2CXP · PDBe 2CXP · UniProt P06745
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.