Structure of PDB 2min Chain A

Receptor sequence
>2minA (length=467) Species: 354 (Azotobacter vinelandii) [Search protein sequence]
SREEVESLIQEVLEVYPEKARKDRNKHLAVNCIISNKKSQPGLMTIRGCA
YAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGTTGVNAFVTMN
FTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDI
ESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKRDED
TTFASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIE
LTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKTIESLRAIA
AKFDESIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHV
IGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFV
KRIKPDLIGSGIKEKFIFQKMGIPFREMHSWDYSGPYHGFDGFAIFARDM
DMTLNNPCWKKLQAPWE
3D structure
PDB2min Redox-dependent structural changes in the nitrogenase P-cluster.
ChainA
Resolution2.03 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) C49 A52 R83 H182
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 CLF A C62 Y64 P85 G87 C88 Y91 C154 G185 C49 Y51 P72 G74 C75 Y78 C141 G172
BS02 CFM A R96 H195 Y229 C275 S278 I355 G356 G357 L358 R359 F381 H442 R83 H182 Y216 C262 S265 I342 G343 G344 L345 R346 F368 H429
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:2min, PDBe:2min, PDBj:2min
PDBsum2min
PubMed9063865
UniProtP07328|NIFD_AZOVI Nitrogenase molybdenum-iron protein alpha chain (Gene Name=nifD)

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