MolNFT v1 · #127113 · protein
Structure of prl-1 in complex with the bateman domain of CNNM2
5MMZ · Metal transporter CNNM2: “Structure of prl-1 in complex with the bateman domain of CNNM2”. X-ray diffraction, 3 pockets (best druggability 0.53). MolNFT v1 #127113 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5MMZ
- Type
- protein
- Length
- 300 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metal transporter CNNM2; Protein tyrosine phosphatase type iva 1
- EC
- 3.1.3.48
- UniProt
- Q3TWN3, Q63739
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metal transporter CNNM2 | protein | 150 | 41% helix, 28% strand | Q3TWN3 |
| B | Protein tyrosine phosphatase type iva 1 (EC 3.1.3.48) | protein | 150 | 43% helix, 17% strand | Q63739 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.53 | 0.77 | 33 | empty |
| 2 | 94 | 0.45 | 0.80 | 16 | empty |
| 3 | 51 | 0.31 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 519 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5MMZ · Structure of PRL-1 in complex with the Bateman domain of CNNM2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q63739 · AlphaFold monomer V2.0 prediction for protein tyrosine phosphatase type iva 1 (Q63739) · a predicted model of the same protein · chain B against A, TM-score 0.98
- Q3TWN3 · AlphaFold monomer V2.0 prediction for metal transporter CNNM2 (Q3TWN3) · a predicted model of the same protein · chain A 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 Q3TWN3
- Every structure of UniProt Q63739
- Elsewhere: RCSB PDB 5MMZ · PDBe 5MMZ · UniProt Q3TWN3 · UniProt Q63739
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