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1aa6
From Proteopedia
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|PDB= 1aa6 |SIZE=350|CAPTION= <scene name='initialview01'>1aa6</scene>, resolution 2.3Å | |PDB= 1aa6 |SIZE=350|CAPTION= <scene name='initialview01'>1aa6</scene>, resolution 2.3Å | ||
|SITE= <scene name='pdbsite=4MO:The+Mo+Atom+Is+Coordinated+To+The+Se+Atom+Of+Sec+140+And+...'>4MO</scene> and <scene name='pdbsite=FS4:The+Fe+S+Cluster+Is+Coordinated+To+The+S+Atoms+Of+CYS+8,+...'>FS4</scene> | |SITE= <scene name='pdbsite=4MO:The+Mo+Atom+Is+Coordinated+To+The+Se+Atom+Of+Sec+140+And+...'>4MO</scene> and <scene name='pdbsite=FS4:The+Fe+S+Cluster+Is+Coordinated+To+The+S+Atoms+Of+CYS+8,+...'>FS4</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=4MO:MOLYBDENUM(IV)+ION'>4MO</scene>, <scene name='pdbligand=CSE:SELENOCYSTEINE'>CSE</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.2 1.2.1.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.2 1.2.1.2] </span> |
|GENE= FDHF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= FDHF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa6 OCA], [http://www.ebi.ac.uk/pdbsum/1aa6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aa6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Boyington, J C.]] | [[Category: Boyington, J C.]] | ||
[[Category: Sun, P D.]] | [[Category: Sun, P D.]] | ||
| - | [[Category: 4MO]] | ||
| - | [[Category: MGD]] | ||
| - | [[Category: SF4]] | ||
[[Category: anaerobic]] | [[Category: anaerobic]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
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[[Category: selenocysteine]] | [[Category: selenocysteine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:36:28 2008'' |
Revision as of 15:36, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , , | ||||||
| Gene: | FDHF (Escherichia coli) | ||||||
| Activity: | Formate dehydrogenase, with EC number 1.2.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REDUCED 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
1AA6 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
Page seeded by OCA on Sun Mar 30 18:36:28 2008
