Structure of PDB 1dy7 Chain A

Receptor sequence

>1dy7A (length=434) Species: 82367 (Paracoccus pantotrophus)

PPEFGMKEMRESWKVHVAPEDRPTQQENDWDLENLFSVTLRDAGQIALID
GATYEIKSVLDTGYAVHISRLSASGRYLFVIGRDGKVNMIDLWMKEPTTV
AEIKIGSEARSIETSKMEGWEDKYAIAGAYWPPQYVIMDGETLEPKKIQS
TRGMTYDEQEYHPEPRVAAILASHYRPEFIVNVKETGKILLVDYTDLDNL
KTTEISAERFLHDGGLDGSHRYFITAANARNKLVVIDTKEGKLVAIEDTG
GQTPHPGRGANFVHPTFGPVWATSHMGDDSVALIGTDPEGHPDNAWKILD
SFPALGGGSLFIKTHPNSQYLYVDATLNPEAEISGSVAVFDIKAMTGDGS
DPEFKTLPIAEWAGITEGQPRVVQGEFNKDGTEVWFSVWNGKDQESALVV
VDDKTLELKHVIKDERLVTPTGKFNVYNTMTDTY

3D structure

• PDB: 1dy7 Proton-Coupled Structural Changes Upon Binding of Carbon Monoxide to Cytochrome Cd(1): A Combined Flash Photolysis and X-Ray Crystallography Study
• Chain: A
• Resolution: 1.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H345 H388
• Catalytic site (residue number reindexed from 1): H212 H255
• 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	R41 H67 I68 R83 R110 S111 Y130 A168 A169 H212 R258 F311 W389 F424

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:1dy7, PDBe:1dy7, PDBj:1dy7
• PDBsum: 1dy7
• PubMed: 10998233
• UniProt: P72181|NIRS_PARPN Nitrite reductase (Gene Name=nirS)