Structure of PDB 4n4k Chain A

Receptor sequence
>4n4kA (length=497) Species: 174633 (Candidatus Kuenenia stuttgartiensis) [Search protein sequence]
GPTFQDVASQVFGQPVGPDNDGTLYIFGLTAKYTEPEYVDGRGPYKSFLK
MLPSIRWYDPEHYWTNGSQTEGVFKNEECVLCHTVQTPTIVNDWKQSSHG
SKDIRRGIGIKKDGKPVEDLVGCADCHGNNHQKLEMPTYKLCNDCHPKET
AEHRAGGLGSHTHAYTVNVLEFSWHVGKPAEEVTGCAHCHAIAENRCSGC
HTRHKFDPAEARKPTACRVCHMGIDHDEWAMYNTSIHGALYEAESARMDW
GKKLKKGNYRVPTCAYCHMQNGDHNPQRFGTIYSDMGMFQVDRGAPKHKA
KRDSWIKLCQDCHSPRFAADKLKEMDAGVNLSFTKWREAAAVIVGCYLDG
VVDPMPEGSAPDWYGHYTFSLLPGGDPRFYATSNLERLGLEMICYLTGNV
YKAYAHMSMYNQTYGNGSAFEQDRKLVEIKTEAAKLRRFAAIEKKIGLEH
KSADFWKHGEYLDLLPGWKRKPGDVDVEWFKRTDIPHRANADAGVEI
3D structure
PDB4n4k Structural Basis of Biological NO Generation by Octaheme Oxidoreductases.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H227 D262 H263 Y451
Catalytic site (residue number reindexed from 1) H190 D225 H226 Y414
Enzyme Commision number 1.7.2.9: hydroxylamine oxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0033740 hydroxylamine oxidoreductase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006809 nitric oxide biosynthetic process
GO:0019331 anaerobic respiration, using ammonium as electron donor
GO:0070207 protein homotrimerization
Cellular Component
GO:0044222 anammoxosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4n4k, PDBe:4n4k, PDBj:4n4k
PDBsum4n4k
PubMed24302732
UniProtQ1PX48|HAO_KUEST Hydroxylamine oxidoreductase (Gene Name=hao)

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