Research workbench
The solution NMR structure of the complex between MNK1 and HAH1 mediated by CU(I)
Analyse The solution NMR structure of the complex between MNK1 and HAH1 mediated by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K1R
- Type
- protein
- Length
- 141 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper-transporting ATPase 1; Copper transport protein ATOX1
- EC
- 3.6.3.4
- UniProt
- Q04656, O00244
- Ligands
- CU
Structure
solution nmr · 2 distinct chains · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper-transporting ATPase 1 (EC 3.6.3.4) | protein | 73 | 23% helix, 32% strand | Q04656 |
| B | Copper transport protein ATOX1 | protein | 68 | 37% helix, 31% strand | O00244 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 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 · 552 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2K1R · The solution NMR structure of the complex between MNK1 and HAH1 mediated by Cu(I) · the same entry in another collection · chain A against A, TM-score 1.00
- O00244 · AlphaFold monomer V2.0 prediction for copper transport protein ATOX1 (O00244) · a predicted model of the same protein · chain B against A, TM-score 0.93
- Q04656 · AlphaFold monomer V2.0 prediction for copper-transporting ATPase 1 (Q04656) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q04656
- Every structure of UniProt O00244
- Elsewhere: RCSB PDB 2K1R · PDBe 2K1R · UniProt Q04656 · UniProt O00244
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