Structure of PDB 6o7q Chain D

Receptor sequence
>6o7qD (length=522) Species: 354 (Azotobacter vinelandii) [Search protein sequence]
SQQVDKIKASYPLFLDQDYKDMLAKKRDGFEEKYPQDKIDEVFQWTTTKE
YQELNFQREALTVNPAKACQPLGAVLCALGFEKTMPYVHGSQGCVAYFRS
YFNRHFREPVSCVSDSMTEDAAVFGGQQNMKDGLQNCKATYKPDMIAVST
TCMAEVIGDDLNAFINNSKKEGFIPDEFPVPFAHTPAFVGSHVTGWDNMF
EGIARYFTLKSMDDKVVGSNKKINIVPGFETYLGNFRVIKRMLSEMGVGY
SLLSDPEEVLDTPADGQFRMYAGGTTQEEMKDAPNALNTVLLQPWHLEKT
KKFVEGTWKHEVPKLNIPMGLDWTDEFLMKVSEISGQPIPASLTKERGRL
VDMMTDSHTWLHGKRFALWGDPDFVMGLVKFLLELGCEPVHILCHNGNKR
WKKAVDAILAASPYGKNATVYIGKDLWHLRSLVFTDKPDFMIGNSYGKFI
QRDTLHKGKEFEVPLIRIGFPIFDRHHLHRSTTLGYEGAMQILTTLVNSI
LERLDEETRGMQATDYNHDLVR
3D structure
PDB6o7q Redox-Dependent Metastability of the Nitrogenase P-Cluster.
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C153 V157
Catalytic site (residue number reindexed from 1) C152 V156
Enzyme Commision number 1.18.6.1: nitrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FE D R108 E109 R107 E108
BS02 CLF D C70 S92 G94 C95 Y98 T152 C153 A188 C69 S91 G93 C94 Y97 T151 C152 A187
BS03 FE D D353 D357 D352 D356
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016163 nitrogenase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
Biological Process
GO:0009399 nitrogen fixation
Cellular Component
GO:0016612 molybdenum-iron nitrogenase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6o7q, PDBe:6o7q, PDBj:6o7q
PDBsum6o7q
PubMed31146522
UniProtP07329|NIFK_AZOVI Nitrogenase molybdenum-iron protein beta chain (Gene Name=nifK)

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