MolNFT v1 · #186177 · protein
Crystal structure of human mitochondrial NAD kinase
7R4L · NAD kinase 2, mitochondrial: “Crystal structure of human mitochondrial NAD kinase”. X-ray diffraction, 2 ligands (NAP, FE), 2 pockets (best druggability 0.54). MolNFT v1 #186177 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 7R4L
- Type
- protein
- Length
- 337 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, FE
- Pockets
- 2 · best druggability 0.54
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 | 337 | 29% helix, 31% strand | Q4G0N4 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- FE · Fe (III) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 245 | 0.54 | 0.76 | 36 | empty |
| 2 | 66 | 0.36 | 0.77 | 20 | empty |
Compared structures
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 7R4L · PDBe 7R4L · UniProt Q4G0N4
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