Structure of PDB 1aof Chain A

Receptor sequence

>1aofA (length=532) Species: 82367 (Paracoccus pantotrophus)

DVAAPGAPEGVTALSDAQYNEANKIYFERCAGCHGVLRKGATGKALTPDL
TRDLGFDYLQSFITYASPAGMPNWGTSGELSAEQVDLMANYLLLDPAAPP
EFGMKEMRESWKVHVAPEDRPTQQMNDWDLENLFSVTLRDAGQIALIDGS
TYEIKTVLDTGYAVHISRLSASGRYLFVIGRDGKVNMIDLWMKEPTTVAE
IKIGSEARSIETSKMEGWEDKYAIAGAYWPPQYVIMDGETLEPKKIQSTR
GMTYDEQEYHPEPRVAAILASHYRPEFIVNVKETGKILLVDYTDLNNLKT
TEISAERFLHDGGLDGSHRYFITAANARNKLVVIDTKEGKLVAIEDTGGQ
TPHPGRGANFVHPTFGPVWATSHMGDDSVALIGTDPEGHPDNAWKILDSF
PALGGGSLFIKTHPNSQYLYVDATLNPEAEISGSVAVFDIKAMTGDGSDP
EFKTLPIAEWAGITEGQPRVVQGEFNKDGTEVWFSVWNGKDQESALVVVD
DKTLELKHVIKDERLVTPTGKFNVYNTMTDTY

3D structure

• PDB: 1aof Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C65 C68 H69 M106 H345 H388
• Catalytic site (residue number reindexed from 1): C30 C33 H34 M71 H310 H353
• Enzyme Commision number: 1.7.2.1: nitrite reductase (NO-forming).
  1.7.99.1: hydroxylamine reductase.

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	HEM	A	C65 C68 H69 G78 L81 Y93 F97 S102 A104 G105 M106 P107 W109	C30 C33 H34 G43 L46 Y58 F62 S67 A69 G70 M71 P72 W74
BS02	DHE	A	R174 H200 I201 R216 R243 S244 Y263 A301 A302 H345 R391 F444 T554 F557	R139 H165 I166 R181 R208 S209 Y228 A266 A267 H310 R356 F409 T519 F522

Gene Ontology

Molecular Function

• GO:0009055 electron transfer activity
• GO:0016491 oxidoreductase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding
• GO:0050418 hydroxylamine reductase activity
• GO:0050421 nitrite reductase (NO-forming) activity

Cellular Component

• GO:0042597 periplasmic space

External links

• PDB: RCSB:1aof, PDBe:1aof, PDBj:1aof
• PDBsum: 1aof
• PubMed: 9311786
• UniProt: P72181|NIRS_PARPN Nitrite reductase (Gene Name=nirS)