1h1l
From Proteopedia
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|PDB= 1h1l |SIZE=350|CAPTION= <scene name='initialview01'>1h1l</scene>, resolution 1.90Å | |PDB= 1h1l |SIZE=350|CAPTION= <scene name='initialview01'>1h1l</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=CT1:Clf+Binding+Site+For+Chain+D'>CT1</scene> | |SITE= <scene name='pdbsite=CT1:Clf+Binding+Site+For+Chain+D'>CT1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CFM:FE-MO-S+CLUSTER'>CFM</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1l OCA], [http://www.ebi.ac.uk/pdbsum/1h1l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h1l RCSB]</span> | ||
}} | }} | ||
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[[Category: Mayer, S M.]] | [[Category: Mayer, S M.]] | ||
[[Category: Smith, B E.]] | [[Category: Smith, B E.]] | ||
| - | [[Category: CFM]] | ||
| - | [[Category: CIT]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: CLF]] | ||
| - | [[Category: MG]] | ||
[[Category: biological nitrogen fixation]] | [[Category: biological nitrogen fixation]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 20:55:49 2008'' |
Revision as of 17:55, 30 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | Nitrogenase, with EC number 1.18.6.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT
Overview
The x-ray crystal structure of NifV(-) Klebsiella pneumoniae nitrogenase MoFe protein (NifV(-) Kp1) has been determined and refined to a resolution of 1.9 A. This is the first structure for a nitrogenase MoFe protein with an altered cofactor. Moreover, it is the first direct evidence that the organic acid citrate is not just present, but replaces homocitrate as a ligand to the molybdenum atom of the iron molybdenum cofactor (FeMoco). Subsequent refinement of the structure revealed that the citrate was present at reduced occupancy.
About this Structure
1H1L is a Protein complex structure of sequences from Klebsiella pneumoniae. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco)., Mayer SM, Gormal CA, Smith BE, Lawson DM, J Biol Chem. 2002 Sep 20;277(38):35263-6. Epub 2002 Jul 19. PMID:12133839
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