2PO5

Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys

Summary for 2PO5

Entry DOI	10.2210/pdb2po5/pdb
Related	1HRK 2PNJ 2PO7
Descriptor	Ferrochelatase, mitochondrial, FE2/S2 (INORGANIC) CLUSTER, CHOLIC ACID, ... (4 entities in total)
Functional Keywords	ferrochelatase; h263c; fe2s2 cluster; heme biosynthesis; protoheme; ferro-lyase; mature length; proteolytically processed mitochondrial inner membrane protein, lyase
Biological source	Homo sapiens (human)
Cellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P22830
Total number of polymer chains	2
Total formula weight	85001.75
Authors	Dailey, H.A.,Wu, C.-K.,Horanyi, P.,Medlock, A.E.,Najahi-Missaoui, A.E.W.,Burden, A.,Dailey, T.A.,Rose, J.P. (deposition date: 2007-04-25, release date: 2007-10-02, Last modification date: 2024-02-21)
Primary citation	Dailey, H.A.,Wu, C.-K.,Horanyi, P.,Medlock, A.E.,Najahi-Missaoui, W.,Burden, A.E.,Dailey, T.A.,Rose, J.P. Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis Biochemistry, 46:7973-7979, 2007 Cited by PubMed: 17567154 DOI: 10.1021/bi700151f PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation