Structure of PDB 1l5h Chain B

Receptor sequence
>1l5hB (length=522) Species: 354 (Azotobacter vinelandii) [Search protein sequence]
SQQVDKIKASYPLFLDQDYKDMLAKKRDGFEEKYPQDKIDEVFQWTTTKE
YQELNFQREALTVNPAKACQPLGAVLCALGFEKTMPYVHGSQGCVAYFRS
YFNRHFREPVSCVSDSMTEDAAVFGGQQNMKDGLQNCKATYKPDMIAVST
TCMAEVIGDDLNAFINNSKKEGFIPDEFPVPFAHTPSFVGSHVTGWDNMF
EGIARYFTLKSMDDKVVGSNKKINIVPGFETYLGNFRVIKRMLSEMGVGY
SLLSDPEEVLDTPADGQFRMYAGGTTQEEMKDAPNALNTVLLQPWHLEKT
KKFVEGTWKHEVPKLNIPMGLDWTDEFLMKVSEISGQPIPASLTKERGRL
VDMMTDSHTWLHGKRFALWGDPDFVMGLVKFLLELGCEPVHILCHNGNKR
WKKAVDAILAASPYGKNATVYIGKDLWHLRSLVFTDKPDFMIGNSYGKFI
QRDTLHKGKEFEVPLIRIGFPIFDRHHLHRSTTLGYEGAMQILTTLVNSI
LERLDEETRGMQATDYNHDLVR
3D structure
PDB1l5h Structure of a cofactor-deficient nitrogenase MoFe protein.
ChainB
Resolution2.3 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 CA B R108 E109 R107 E108
BS02 CLF B C70 P72 S92 G94 C95 Y98 T152 C153 S188 C69 P71 S91 G93 C94 Y97 T151 C152 S187
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:1l5h, PDBe:1l5h, PDBj:1l5h
PDBsum1l5h
PubMed11951047
UniProtP07329|NIFK_AZOVI Nitrogenase molybdenum-iron protein beta chain (Gene Name=nifK)

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