Structure of PDB 5bvh Chain A

Receptor sequence

>5bvhA (length=477) Species: 354 (Azotobacter vinelandii)

MSREEVESLIQEVLEVYPEKARKDRNKHLAVNDPAVTQSKKCIISNKKSQ
PGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGT
TGVNAFVTMNFTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSE
CPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVR
DWVLGKRDEDTTFASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQW
SGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPT
KTIESLRAIAAKFDESIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVML
YIGGLRPRHVIGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDD
VTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFRQMHSWDYSGPYHGF
DGFAIFARDMDMTLNNPCWKKLQAPWE

3D structure

• PDB: 5bvh Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor.
• Chain: A
• Resolution: 1.53 Å

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	ICS	A	V70 R96 Y229 C275 S278 I355 G356 G357 L358 R359 F381 H442	V67 R93 Y226 C272 S275 I352 G353 G354 L355 R356 F378 H439
BS02	ICH	A	V70 R96 H195 Y229 I231 C275 S278 I355 G356 G357 L358 R359 F381 H442	V67 R93 H192 Y226 I228 C272 S275 I352 G353 G354 L355 R356 F378 H439
BS03	CLF	A	C62 Y64 G87 C88 Y91 C154 G185	C59 Y61 G84 C85 Y88 C151 G182

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

External links

• PDB: RCSB:5bvh, PDBe:5bvh, PDBj:5bvh
• PDBsum: 5bvh
• PubMed: 26673079
• UniProt: P07328|NIFD_AZOVI Nitrogenase molybdenum-iron protein alpha chain (Gene Name=nifD)