Structure of PDB 1n15 Chain A

Receptor sequence

>1n15A (length=538) Species: 287 (Pseudomonas aeruginosa)

AAEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQRCAGCHGVLR
KGATGKPLTPDITQQRGQQYLEALITYGTPLGMPNWGSSGELSKEQITLM
AKYIQHTPPQPPEWGMPEMRESWKVLVKPEDRPKKQLNDLDLPNLFSVTL
RDAGQIALVDGDSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMI
DLWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYWPPQFAIMDG
ETLEPKQIVSTRGMTVDTQTYHPEPRVAAIIASHEHPEFIVNVKETGKVL
LVNYKDIDNLTVTSIGAAPFLHDGGWDSSHRYFMTAANNSNKVAVIDSKD
RRLSALVDVGKTPHPGRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNH
PQYAWKKVAELQGQGGGSLFIKTHPKSSHLYVDTTFNPDARISQSVAVFD
LKNLDAKYQVLPIAEWADLGEGAKRVVQPEYNKRGDEVWFSVWNGKNDSS
ALVVVDDKTLKLKAVVKDPRLITPTGKFNVYNTQHDVY

3D structure

• PDB: 1n15 Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase?
• Chain: A
• Resolution: 2.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C47 C50 H51 M88 H327 H369
• Catalytic site (residue number reindexed from 1): C42 C45 H46 M83 H322 H364
• 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	HEC	A	C47 C50 H51 T59 L63 R71 L79 I80 T84 L86 M88 P89 W91	C42 C45 H46 T54 L58 R66 L74 I75 T79 L81 M83 P84 W86
BS02	DHE	A	R156 H182 I183 R185 R198 R225 S226 Y245 A283 A284 H327 R372 F425 Q483 F533	R151 H177 I178 R180 R193 R220 S221 Y240 A278 A279 H322 R367 F420 Q478 F528

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:1n15, PDBe:1n15, PDBj:1n15
• PDBsum: 1n15
• PubMed: 10329702
• UniProt: P24474|NIRS_PSEAE Nitrite reductase (Gene Name=nirS)