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: 17567154DOI: 10.1021/bi700151f PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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