Research workbench
Mutant P9L of adenylate kinase from E. COLI, modified in the gly-loop
Analyse Mutant P9L of adenylate kinase from E. COLI, modified in the gly-loop in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E4Y
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylate kinase
- EC
- 2.7.4.3
- UniProt
- P69441
- Ligands
- AP5
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Adenylate kinase (EC 2.7.4.3) | protein | 214 | 50% helix, 17% strand | P69441 |
Ligands and binding sites
- AP5 · Bis(adenosine)-5'-pentaphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 666 | 0.84 | 0.88 | 80 | AP5 |
| 2 | 570 | 0.83 | 0.89 | 65 | AP5 |
| 3 | 50 | 0.43 | 0.84 | 13 | empty |
| 4 | 63 | 0.29 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 567 Ų buried · 2 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 P69441
- Elsewhere: RCSB PDB 1E4Y · PDBe 1E4Y · UniProt P69441
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