1fdo | pdb_00001fdo
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| 1fdo, resolution 2.8Å | |||||||||||||
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| Sites: | FS4 and MO4 | ||||||||||||
| Ligands: | SF4, MGD and 6MO | ||||||||||||
| Gene: | FDHF (Escherichia coli) | ||||||||||||
| Activity: | Formate dehydrogenase, with EC number 1.2.1.2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI
Overview
Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbon dioxide. The crystal structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate dehydrogenase H (with and without bound inhibitor) and the reduced [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain alphabeta structure with the molybdenum directly coordinated to selenium and both MGD cofactors. These structures suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer.
About this Structure
1FDO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster., Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD, Science. 1997 Feb 28;275(5304):1305-8. PMID:9036855
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