Structure of PDB 6tpo Chain A

Receptor sequence
>6tpoA (length=523) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
HVVRTNGAPDMSESEFNEAKQIYFQRCAGCHGVLRKGATGKPLTPDITQQ
RGQQYLEALITYGTPLGMPNWGSSGELSKEQITLMAKYIQHTPPQPPEWG
MPEMRESWKVLVKPEDRPKKQLNDLDLPNLFSVTLRDAGQIALVDGDSKK
IVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMIDLWAKEPTKVAEIKI
GIEARSVESSKFKGYEDRYTIAGAYWPPQFAIMDGETLEPKQIVSTRGMT
VDTQTYHPEPRVAAIIASHEHPEFIVNVKETGKVLLVNYKDIDNLTVTSI
GAAPFLHDGGWDSSHRYFMTAANNSNKVAVIDSKDRRLSALVDVGKTPHP
GRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNHPQYAWKKVAELQGQG
GGSLFIKTHPKSSHLYVDTTFNPDARISQSVAVFDLKNLDAKYQVLPIAE
WADLGEGAKRVVQPEYNKRGDEVWFSVWNGKNDSSALVVVDDKTLKLKAV
VKDPRLITPTGKFNVYNTQHDVY
3D structure
PDB6tpo Structure of heme d 1 -free cd 1 nitrite reductase NirS.
ChainA
Resolution1.861 Å
3D
structure
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Enzymatic activity
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 G60 K61 L63 R71 Y75 T84 G87 M88 P89 W91 C27 C30 H31 G40 K41 L43 R51 Y55 T64 G67 M68 P69 W71
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:6tpo, PDBe:6tpo, PDBj:6tpo
PDBsum6tpo
PubMed32510465
UniProtP24474|NIRS_PSEAE Nitrite reductase (Gene Name=nirS)

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