Research workbench
Adenylate kinase from methanococcus thermolithotrophicus
Analyse Adenylate kinase from methanococcus thermolithotrophicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KI9
- Type
- protein
- Length
- 575 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylate kinase
- EC
- 2.7.4.3
- UniProt
- P43410
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylate kinase (EC 2.7.4.3) | protein | 191 | 50% helix, 17% strand | P43410 |
| B, C | Adenylate kinase (EC 2.7.4.3) | protein | 192 | 47% helix, 18% strand | P43410 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 560 | 0.65 | 0.76 | 54 | empty |
| 2 | 486 | 0.61 | 0.75 | 40 | empty |
| 3 | 333 | 0.55 | 0.75 | 44 | empty |
| 4 | 124 | 0.49 | 0.80 | 21 | empty |
| 5 | 134 | 0.39 | 0.74 | 31 | empty |
Interfaces
3 interfaces between chains.
- A–B · 786 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 754 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 750 Ų buried · 6 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 P43410
- Elsewhere: RCSB PDB 1KI9 · PDBe 1KI9 · UniProt P43410
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