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Ligands
Code Name Style Show Link
CA Calcium ion
CFN Fe(7)-mo-S(9)-N cluster
CLF Fe(8)-S(7) cluster
HCA 3-hydroxy-3-carboxy-adipic acid
Non-standard Residues
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Code : 3K1A   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha-70Ile MoFe protein variant
Release Data : 2010-02-16
Compound :
mol_id molecule chains synonym
1 Nitrogenase molybdenum-iron protein alpha chain A,C Nitrogenase component I, Dinitrogenase
ec: 1.18.6.1
mutation: V70I
mol_id molecule chains synonym
2 Nitrogenase molybdenum-iron protein beta chain B,D Nitrogenase component I, Dinitrogenase
ec: 1.18.6.1
Source :
mol_id organism_scientific expression_system
1 Azotobacter vinelandii  (taxid:354) Escherichia coli  (taxid:562)
gene: nifDK, nifK
mol_id organism_scientific expression_system
2 Azotobacter vinelandii  (taxid:354) Escherichia coli  (taxid:562)
gene: nifD
Authors : Peters, J.W., Sarma, R., Barney, B.M., Keable, S., Seefeldt, L.C., Dean, D.R.
Keywords : NITROGEN FIXATION, MoFe protein, nitrogenase, isoleucine, proton reduction, nitrogen, acetylene, hydride reduction, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, Oxidoreductase, Molybdenum
Exp. method : X-RAY DIFFRACTION ( 2.23 Å )
Citation :

Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha-70(Ile) MoFe protein variant

Sarma, R.,Barney, B.M.,Keable, S.  et al.
(2010)  J.Inorg.Biochem.  104 : 385 - 389

PubMed: 20022118
DOI: 10.1016/j.jinorgbio.2009.11.009

Chain : A, C
UniProt : P07328 (NIFD_AZOVI)
Reaction: EC: Evidence:
Physiological Direction:
16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate 1.18.6.1 -
-
Chain : B, D
UniProt : P07329 (NIFK_AZOVI)
Reaction: EC: Evidence:
Physiological Direction:
16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate 1.18.6.1 -
-