MolNFT v1 · #27534 · protein

Crystal structure of human DELTAF508 human NBD1 domain with ATP

1XMJ · Cystic fibrosis transmembrane conductance regulator: “Crystal structure of human DELTAF508 human NBD1 domain with ATP”. X-ray diffraction, 2 ligands (ATP, MG), 1 pocket (best druggability 0.48). MolNFT v1 #27534 on GenesisL1: 3D…

PDB: 1XMJ
Type: protein
Length: 246 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cystic fibrosis transmembrane conductance regulator
EC: 3.6.3.49
UniProt: P13569
Ligands: ATP, MG
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49)	protein	246	39% helix, 23% strand	P13569

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	168	0.48	0.77	34	MG, ATP

Compared structures

1XMJ · Crystal structure of human deltaF508 human NBD1 domain with ATP · the same entry in another collection · chain A against A, TM-score 1.00
P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P13569
Elsewhere: RCSB PDB 1XMJ · PDBe 1XMJ · UniProt P13569

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