MolNFT v1 · #47491 · protein
Structure of the N-terminally truncated pas domain of signal transduction histidine kinase from nostoc punctiforme pcc 73102 with homology to the H-NOXA/H-noba domain of the soluble guanylyl cyclase
2P08: “Structure of the N-terminally truncated pas domain of signal transduction histidine kinase from nostoc…”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.31). MolNFT v1 #47491 on GenesisL1: 3D structure, binding…
- PDB
- 2P08
- Type
- protein
- Length
- 217 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal transduction histidine kinase
- EC
- 2.7.3.-
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal transduction histidine kinase (EC 2.7.3.-) | protein | 107 | 20% helix, 34% strand | — |
| B | Signal transduction histidine kinase (EC 2.7.3.-) | protein | 110 | 16% helix, 32% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.31 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 937 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2P08 · Structure of the N-terminally truncated PAS domain of signal transduction histidine… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 2P08 · PDBe 2P08
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