4C3Z

Nucleotide-free crystal structure of nucleotide-binding domain 1 from human MRP1 supports a general-base catalysis mechanism for ATP hydrolysis.

Summary for 4C3Z

Entry DOI	10.2210/pdb4c3z/pdb
Descriptor	MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN 1, SULFATE ION (3 entities in total)
Functional Keywords	transport protein, atp-binding cassette transporters, multidrug resistance protein 1, general-base mechanism
Biological source	HOMO SAPIENS (HUMAN)
Cellular location	Cell membrane ; Multi-pass membrane protein : P33527
Total number of polymer chains	1
Total formula weight	29609.17
Authors	Chaptal, V.,Gueguen-Chaignon, V.,Magnard, S.,Falson, P.,Di Pietro, A.,Baubichon-Cortay, H. (deposition date: 2013-08-28, release date: 2014-09-10, Last modification date: 2023-12-20)
Primary citation	Chaptal, V.,Magnard, S.,Gueguen-Chaignon, V.,Falson, P.,Di Pietro, A.,Baubichon-Cortay, H. Nucleotide-Free Crystal Structure of Nucleotide-Binding Domain 1 from Human Abcc1 Supports a 'General-Base Catalysis' Mechanism for ATP Hydrolysis. Biochem.Pharm., 3:150-, 2014 Cited by DOI: 10.4172/2167-0501.1000150 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation