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Crystal structure of the cytosolic domain of human CNNM3

Analyse Crystal structure of the cytosolic domain of human CNNM3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MN6
Type: protein
Length: 590 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metal transporter CNNM3
UniProt: Q8NE01
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metal transporter CNNM3	protein	293	31% helix, 26% strand	Q8NE01
B	Metal transporter CNNM3	protein	297	31% helix, 27% strand	Q8NE01

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	94	0.77	0.97	22	empty
2	132	0.61	0.85	23	empty
3	240	0.58	0.79	26	empty
4	71	0.49	0.84	13	empty
5	148	0.47	0.77	20	empty

Interfaces

1 interface between chains.

A–B · 3594 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

6MN6 · Crystal structure of the cytosolic domain of human CNNM3 · the same entry in another collection · chain A against A, TM-score 1.00
Q8NE01 · AlphaFold monomer V2.0 prediction for metal transporter CNNM3 (Q8NE01) · a predicted model of the same protein · chain B against A, TM-score 0.54

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 Q8NE01
Elsewhere: RCSB PDB 6MN6 · PDBe 6MN6 · UniProt Q8NE01

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