MolNFT v1 · #146368 · protein

Crystal structure of CNNM3 cyclic nucleotide-binding homology domain

6DFD · Metal transporter CNNM3: “Crystal structure of CNNM3 cyclic nucleotide-binding homology domain”. X-ray diffraction, 2 pockets (best druggability 0.33). MolNFT v1 #146368 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6DFD
Type: protein
Length: 262 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metal transporter CNNM3
UniProt: Q8NE01
Pockets: 2 · best druggability 0.33

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metal transporter CNNM3	protein	137	34% helix, 29% strand	Q8NE01
B	Metal transporter CNNM3	protein	125	33% helix, 30% strand	Q8NE01

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.33	0.76	16	empty
2	68	0.32	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 772 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

6DFD · Crystal structure of CNNM3 cyclic nucleotide-binding homology domain · 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 A against A, TM-score 0.96

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 6DFD · PDBe 6DFD · UniProt Q8NE01

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