Structure of PDB 1m1y Chain I

Receptor sequence
>1m1yI (length=477) Species: 354 (Azotobacter vinelandii) [Search protein sequence]
MSREEVESLIQEVLEVYPEKARKDRNKHLAVNDPAVTQSKKCIISNKKSQ
PGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGT
TGVNAFVTMNFTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSE
CPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVR
DWVLGKRDEDTTFASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQW
SGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPT
KTIESLRAIAAKFDESIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVML
YIGGLRPRHVIGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDD
VTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSWDYSGPYHGF
DGFAIFARDMDMTLNNPCWKKLQAPWE
3D structure
PDB1m1y Biochemical and Structural Characterization of the Crosslinked Complex of Nitrogenase: Comparison to the ADP-AlF4- Stabilized Structure
ChainI
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C62 A65 R96 H195
Catalytic site (residue number reindexed from 1) C59 A62 R93 H192
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 CFM I R96 H195 Y229 I231 C275 S278 I355 G356 G357 L358 F381 H442 R93 H192 Y226 I228 C272 S275 I352 G353 G354 L355 F378 H439
BS02 CLF I C62 Y64 G87 C88 E153 C154 C59 Y61 G84 C85 E150 C151
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:1m1y, PDBe:1m1y, PDBj:1m1y
PDBsum1m1y
PubMed12501184
UniProtP07328|NIFD_AZOVI Nitrogenase molybdenum-iron protein alpha chain (Gene Name=nifD)

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