Structure of PDB 1n2c Chain E

Receptor sequence
>1n2cE (length=274) Species: 354 (Azotobacter vinelandii) [Search protein sequence]
AMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILH
SKAQNTIMEMAAEAGTVEDLELEDVLKAGYGGVKCVESGGPEPGVGCAGR
GVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIV
CSGEMMAMYAANNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALA
NKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRALARKVVDN
KLLVIPNPITMDELEELLMEFGIM
3D structure
PDB1n2c Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction.
ChainE
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K10 G12 K15 K41 D129
Catalytic site (residue number reindexed from 1) K10 G12 K15 K41 D129
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 MG E S16 D39 D43 S16 D39 D43
BS02 ALF E G12 K15 D39 G128 G12 K15 D39 G128
BS03 ADP E G12 G14 K15 S16 T17 N185 R213 D214 V217 Q218 E221 G12 G14 K15 S16 T17 N185 R213 D214 V217 Q218 E221
BS04 SF4 E C97 G99 V131 C132 C97 G99 V131 C132
BS05 ADP E K10 E154 M156 K10 E154 M156
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016163 nitrogenase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0009399 nitrogen fixation

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Molecular Function
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Biological Process
External links
PDB RCSB:1n2c, PDBe:1n2c, PDBj:1n2c
PDBsum1n2c
PubMed9163420
UniProtP00459|NIFH1_AZOVI Nitrogenase iron protein 1 (Gene Name=nifH1)

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