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Structure of human adenylate kinase 2
Analyse Structure of human adenylate kinase 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C9Y
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylate kinase isoenzyme 2, mitochondrial
- EC
- 2.7.4.3
- UniProt
- P54819
- Ligands
- B4P
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylate kinase isoenzyme 2, mitochondrial (EC 2.7.4.3) | protein | 218 | 50% helix, 17% strand | P54819 |
Ligands and binding sites
- B4P · Bis(adenosine)-5'-tetraphosphate · ligand · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 170 | 0.49 | 0.77 | 23 | B4P |
| 2 | 72 | 0.35 | 0.77 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P54819
- Elsewhere: RCSB PDB 2C9Y · PDBe 2C9Y · UniProt P54819
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