MolNFT v1 · #95700 · protein

Structural and ligand binding properties of the bateman domain of human magnesium transporters CNNM2 and CNNM4

4IY2 · Metal transporter CNNM2: “Structural and ligand binding properties of the bateman domain of human magnesium transporters CNNM2 and CNNM4”. X-ray diffraction, 2 pockets (best druggability 0.63). MolNFT v1 #95700 on GenesisL1: 3D…

PDB: 4IY2
Type: protein
Length: 304 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metal transporter CNNM2
UniProt: Q9H8M5
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Metal transporter CNNM2	protein	152	40% helix, 27% strand	Q9H8M5

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	536	0.63	0.75	50	empty
2	58	0.51	0.87	16	empty

Interfaces

1 interface between chains.

A–C · 1400 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

4IY2 · Structural and ligand binding properties of the Bateman domain of human magnesium… · the same entry in another collection · chain A against A, TM-score 1.00
Q9H8M5 · AlphaFold monomer V2.0 prediction for metal transporter CNNM2 (Q9H8M5) · 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 Q9H8M5
Elsewhere: RCSB PDB 4IY2 · PDBe 4IY2 · UniProt Q9H8M5

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