Structure of PDB 1aom Chain A

Receptor sequence

>1aomA (length=439) Species: 82367 (Paracoccus pantotrophus)

LDPAAPPEFGMKEMRESWKVHVAPEDRPTQQMNDWDLENLFSVTLRDAGQ
IALIDGSTYEIKTVLDTGYAVHISRLSASGRYLFVIGRDGKVNMIDLWMK
EPTTVAEIKIGSEARSIETSKMEGWEDKYAIAGAYWPPQYVIMDGETLEP
KKIQSTRGMTYDEQEYHPEPRVAAILASHYRPEFIVNVKETGKILLVDYT
DLNNLKTTEISAERFLHDGGLDGSHRYFITAANARNKLVVIDTKEGKLVA
IEDTGGQTPHPGRGANFVHPTFGPVWATSHMGDDSVALIGTDPEGHPDNA
WKILDSFPALGGGSLFIKTHPNSQYLYVDATLNPEAEISGSVAVFDIKAM
TGDGSDPEFKTLPIAEWAGITEGQPRVVQGEFNKDGTEVWFSVWNGKDQE
SALVVVDDKTLELKHVIKDERLVTPTGKFNVYNTMTDTY

3D structure

• PDB: 1aom Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H345 H388
• Catalytic site (residue number reindexed from 1): H217 H260
• 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	DHE	A	R174 H200 I201 R216 R243 S244 Y263 A301 A302 H345 R391 F444 W522 F557	R46 H72 I73 R88 R115 S116 Y135 A173 A174 H217 R263 F316 W394 F429

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