Structure of PDB 4d02 Chain A

Receptor sequence
>4d02A (length=399) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SIVVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTV
DHKFSREFVQNLRNEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIY
CTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDS
MMTYLTGDAVLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTP
FSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVELYLKWAADYQE
DRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILTN
VFRSKGVLVGTSTMNNVMMPKIAGLVEEMTGLRFRNKRASAFGSHGWSGG
AVDRLSTRLQDAGFEMSLSLKAKWRPDQDALKLCREHGREIARQWALAP
3D structure
PDB4d02 Structure of Escherichia Coli Flavodiiron Nitric Oxide Reductase.
ChainA
Resolution1.755 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H23 H79 E81 D83 H147 D166 Y194 H227
Catalytic site (residue number reindexed from 1) H22 H78 E80 D82 H146 D165 Y193 H226
Enzyme Commision number ?
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0009055 electron transfer activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016661 oxidoreductase activity, acting on other nitrogenous compounds as donors
GO:0016966 nitric oxide reductase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0046210 nitric oxide catabolic process
GO:0071731 response to nitric oxide
Cellular Component
GO:0005737 cytoplasm
GO:0032991 protein-containing complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4d02, PDBe:4d02, PDBj:4d02
PDBsum4d02
PubMed27725182
UniProtQ46877|NORV_ECOLI Anaerobic nitric oxide reductase flavorubredoxin (Gene Name=norV)

[Back to BioLiP]