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Crystal structure of human AK4(L171P)
Analyse Crystal structure of human AK4(L171P) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NDP
- Type
- protein
- Length
- 420 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylate kinase isoenzyme 4
- EC
- 2.7.4.3
- UniProt
- P27144
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylate kinase isoenzyme 4 (EC 2.7.4.3) | protein | 214 | 40% helix, 16% strand | P27144 |
| B | Adenylate kinase isoenzyme 4 (EC 2.7.4.3) | protein | 206 | 39% helix, 19% strand | P27144 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 897 | 0.80 | 0.83 | 127 | SO4 |
| 2 | 100 | 0.47 | 0.80 | 21 | empty |
| 3 | 90 | 0.45 | 0.80 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 588 Ų buried · 10 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 P27144
- Elsewhere: RCSB PDB 3NDP · PDBe 3NDP · UniProt P27144
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