Research workbench
Structure of mntr E11K mutant complexed with CD2+
Analyse Structure of mntr E11K mutant complexed with CD2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HX7
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator mntr
- UniProt
- P54512
- Ligands
- CD
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator mntr | protein | 128 | 80% helix, 2% strand | P54512 |
| B | Transcriptional regulator mntr | protein | 130 | 78% helix, 3% strand | P54512 |
Ligands and binding sites
- CD · Cadmium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1325 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4HX7 · Structure of MNTR E11K mutant complexed with Cd2+ · the same entry in another collection · chain A against A, TM-score 1.00
- P54512 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator mntr (P54512) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P54512
- Elsewhere: RCSB PDB 4HX7 · PDBe 4HX7 · UniProt P54512
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.