MolNFT v1 · #166244 · protein
Crystal structure of nucleotide-binding domain 2 (NBD2) of the human cystic fibrosis transmembrane conductance regulator (cftr)
6UK1: “Crystal structure of nucleotide-binding domain 2 (NBD2) of the human cystic fibrosis transmembrane…”. X-ray diffraction, 2 ligands (ATP, MG). MolNFT v1 #166244 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UK1
- Type
- protein
- Length
- 912 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13569
- Ligands
- ATP, MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 229 | — | P13569 |
| B | — | protein | 228 | — | P13569 |
| D | — | protein | 226 | — | P13569 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, D, B, C
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UK1 · Crystal structure of nucleotide-binding domain 2 (NBD2) of the human Cystic Fibrosis… · the same entry in another collection · chain D against D, TM-score 1.00
- P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain C against A, TM-score 0.86
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 6UK1 · PDBe 6UK1 · UniProt P13569
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