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1h0h
From Proteopedia
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|PDB= 1h0h |SIZE=350|CAPTION= <scene name='initialview01'>1h0h</scene>, resolution 1.80Å | |PDB= 1h0h |SIZE=350|CAPTION= <scene name='initialview01'>1h0h</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=WA:Fs4+Binding+Site+For+Chain+L'>WA</scene> | |SITE= <scene name='pdbsite=WA:Fs4+Binding+Site+For+Chain+L'>WA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=2MD:GUANYLATE-O | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=2MD:GUANYLATE-O'-PHOSPHORIC+ACID+MONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,5,6,7,8A,9,10,10A-OCTAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)+ESTER'>2MD</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=S:SULFUR+ATOM'>S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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[[Category: tungsten selenium formate dehydrogenase]] | [[Category: tungsten selenium formate dehydrogenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:01:09 2008'' |
Revision as of 10:01, 23 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | , , , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TUNGSTEN CONTAINING FORMATE DEHYDROGENASE FROM DESULFOVIBRIO GIGAS
Overview
Desulfovibrio gigas formate dehydrogenase is the first representative of a tungsten-containing enzyme from a mesophile that has been structurally characterized. It is a heterodimer of 110 and 24 kDa subunits. The large subunit, homologous to E. coli FDH-H and to D. desulfuricans nitrate reductase, harbors the W site and one [4Fe-4S] center. No small subunit ortholog containing three [4Fe-4S] clusters has been reported. The structural homology with E. coli FDH-H shows that the essential residues (SeCys158, His159, and Arg407) at the active site are conserved. The active site is accessible via a positively charged tunnel, while product release may be facilitated, for H(+) by buried waters and protonable amino acids and for CO(2) through a hydrophobic channel.
About this Structure
1H0H is a Protein complex structure of sequences from Desulfovibrio gigas. Full crystallographic information is available from OCA.
Reference
Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas., Raaijmakers H, Macieira S, Dias JM, Teixeira S, Bursakov S, Huber R, Moura JJ, Moura I, Romao MJ, Structure. 2002 Sep;10(9):1261-72. PMID:12220497
Page seeded by OCA on Sun Mar 23 12:01:09 2008
