MolNFT v1 · #29710 · protein
Crystal structure of the MG+2/BEF3-bound receiver domain of kdp potassium transport system response regulator kdpe
1ZH4 · Kdp operon transcriptional regulatory protein kdpe: “Crystal structure of the MG+2/BEF3-bound receiver domain of kdp potassium transport system response regulator…”. X-ray diffraction, 2 ligands (BEF, MG), 2 pockets (best…
- PDB
- 1ZH4
- Type
- protein
- Length
- 241 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kdp operon transcriptional regulatory protein kdpe
- UniProt
- P21866
- Ligands
- BEF, MG
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kdp operon transcriptional regulatory protein kdpe | protein | 121 | 45% helix, 22% strand | P21866 |
| B | Kdp operon transcriptional regulatory protein kdpe | protein | 120 | 48% helix, 23% strand | P21866 |
Ligands and binding sites
- BEF · Beryllium trifluoride ion · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.73 | 0.95 | 20 | empty |
| 2 | 86 | 0.38 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 988 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 1ZH4 · Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport… · the same entry in another collection · chain A against A, TM-score 1.00
- P21866 · AlphaFold monomer V2.0 prediction for kdp operon transcriptional regulatory protein kdpe… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P21866
- Elsewhere: RCSB PDB 1ZH4 · PDBe 1ZH4 · UniProt P21866
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