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Crystal structure of mitochondrial NAD kinase

Analyse Crystal structure of mitochondrial NAD kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7R4M
Type: protein
Length: 338 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD kinase 2, mitochondrial
EC: 2.7.1.23
UniProt: Q4G0N4
Ligands: NAP, CA
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD kinase 2, mitochondrial (EC 2.7.1.23)	protein	338	29% helix, 31% strand	Q4G0N4

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	197	0.52	0.78	30	CA
2	71	0.39	0.78	20	empty
3	58	0.38	0.80	12	empty

Compared structures

7R4M · Crystal structure of mitochondrial NAD kinase · the same entry in another collection · chain A against A, TM-score 1.00
Q4G0N4 · AlphaFold monomer V2.0 prediction for NAD kinase 2, mitochondrial (Q4G0N4) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q4G0N4
Elsewhere: RCSB PDB 7R4M · PDBe 7R4M · UniProt Q4G0N4

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