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

Analyse Structural and ligand binding properties of the bateman domain of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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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