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2PNJ

Crystal structure of human ferrochelatase mutant with Phe 337 replaced by Ala

Summary for 2PNJ
Entry DOI10.2210/pdb2pnj/pdb
Related1HRK 2PO5 2PO7
DescriptorFerrochelatase, mitochondrial, FE2/S2 (INORGANIC) CLUSTER, CHOLIC ACID, ... (4 entities in total)
Functional Keywordsferrochelatase; f337a mutant; fe2s2 cluster; heme biosynthesis; protoheme ferro-lyase; mature length; proteolytically processed mitochondrial inner membrane protein, lyase
Biological sourceHomo sapiens (human)
Cellular locationMitochondrion inner membrane; Peripheral membrane protein; Matrix side: P22830
Total number of polymer chains2
Total formula weight84919.57
Authors
Dailey, H.A.,Wu, C.-K.,Horanyi, P.,Medlock, A.E.,Najahi-Missaoui, W.,Burden, A.E.,Dailey, T.A.,Rose, J.P. (deposition date: 2007-04-24, release date: 2007-10-02, Last modification date: 2023-08-30)
Primary citationDailey, 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 (2.35 Å)
Structure validation

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