MolNFT v1 · #124004 · protein
Crystal structure of the complex between phosphatase prl-2 in the oxidized state with the bateman domain of murine magnesium transporter CNNM3
5K24: “Crystal structure of the complex between phosphatase prl-2 in the oxidized state with the bateman domain of…”. X-ray diffraction. MolNFT v1 #124004 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5K24
- Type
- protein
- Length
- 573 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O70274, Q32NY4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 152 | — | O70274 |
| B | — | protein | 149 | — | O70274 |
| C | — | protein | 137 | — | Q32NY4 |
| D | — | protein | 135 | — | Q32NY4 |
Ligands and binding sites
- FLC · Citrate anion · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5K24 · Crystal structure of the complex between phosphatase PRL-2 in the oxidized state with the… · the same entry in another collection · chain D against D, TM-score 1.00
- O70274 · AlphaFold monomer V2.0 prediction for protein tyrosine phosphatase type iva 2 (O70274) · a predicted model of the same protein · chain B against A, TM-score 0.97
- Q32NY4 · AlphaFold monomer V2.0 prediction for metal transporter CNNM3 (Q32NY4) · a predicted model of the same protein · chain C against A, TM-score 0.97
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 O70274
- Every structure of UniProt Q32NY4
- Elsewhere: RCSB PDB 5K24 · PDBe 5K24 · UniProt O70274 · UniProt Q32NY4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.