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NME2 bound to myristoyl-CoA

Analyse NME2 bound to myristoyl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KPF
Type: protein
Length: 874 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P22392
Ligands: WYV, MG

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	—	protein	152	—	P22392
D	—	protein	142	—	P22392
E	—	protein	141	—	P22392
F	—	protein	135	—	P22392

Ligands and binding sites

WYV · Myristoyl coenzyme A · ligand · 3 copies · chains A, B, C
MG · Magnesium ion · metal · 7 copies · chains B, D, E, F
GOL · Glycerol · additive · chains D

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

Compared structures

7KPF · NME2 bound to myristoyl-CoA · the same entry in another collection · chain F against F, TM-score 1.00
P22392 · AlphaFold monomer V2.0 prediction for nucleoside diphosphate kinase B (P22392) · a predicted model of the same protein · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P22392
Elsewhere: RCSB PDB 7KPF · PDBe 7KPF · UniProt P22392

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