Research workbench
Crystal structure of the wild-type hupr receiver domain
Analyse Crystal structure of the wild-type hupr receiver domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JK1
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydrogenase transcriptional regulatory protein HUPR1
- UniProt
- P26408
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydrogenase transcriptional regulatory protein HUPR1 | protein | 138 | 52% helix, 19% strand | P26408 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2JK1 · Crystal structure of the wild-type HupR receiver domain · the same entry in another collection · chain A against A, TM-score 1.00
- P26408 · AlphaFold monomer V2.0 prediction for hydrogenase transcriptional regulatory protein… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P26408
- Elsewhere: RCSB PDB 2JK1 · PDBe 2JK1 · UniProt P26408
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