Structure of PDB 4b65 Chain A

Receptor sequence
>4b65A (length=456) Species: 746128 (Aspergillus fumigatus) [Search protein sequence]
PRLRSTPQDELHDLLCVGFGPASLAIAIALHDALDPRLNKSASNIHAQPK
ICFLERQKQFAWHSGMLVPGSKMQISFIKDLATLRDPRSSFTFLNYLHQK
GRLIHFTNLSTFLPARLEFEDYMRWCAQQFSDVVAYGEEVVEVIPGKSDP
SSSVVDFFTVRSRNVETGEISARRTRKVVIAIGGTAKMPSGLPQDPRIIH
SSKYCTTLPALLKDKSKPYNIAVLGSGQSAAEIFHDLQKRYPNSRTTLIM
RDSAMRPSDDSPFVNEIFNPERVDKFYSQSAAERQRSLLADKATNYSVVR
LELIEEIYNDMYLQRVKNPDETQWQHRILPERKITRVEHHGPQSRMRIHL
KSSKPEVKETLEVDALMVATGYNRNAHERLLSKVQHLRPTGQDQWKPHRD
YRVEMDPSKVSSEAGIWLQGCNERTHGLSDSLLSVLAVRGGEMVQSIFGE
QLERAA
3D structure
PDB4b65 Structural Insight Into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases.
ChainA
Resolution2.32 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.13.196: L-ornithine N(5)-monooxygenase [NAD(P)H].
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004497 monooxygenase activity
GO:0004499 N,N-dimethylaniline monooxygenase activity
GO:0005506 iron ion binding
GO:0031172 ornithine N5-monooxygenase activity
GO:0070401 NADP+ binding
Biological Process
GO:0006696 ergosterol biosynthetic process
GO:0006879 intracellular iron ion homeostasis
GO:0009058 biosynthetic process
GO:0010106 cellular response to iron ion starvation
GO:0019290 siderophore biosynthetic process
GO:0031169 ferrichrome biosynthetic process
GO:0033214 siderophore-dependent iron import into cell
GO:0044550 secondary metabolite biosynthetic process
Cellular Component
GO:0005575 cellular_component

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4b65, PDBe:4b65, PDBj:4b65
PDBsum4b65
PubMed22928747
UniProtE9QYP0|SIDA_ASPFU L-ornithine N(5)-monooxygenase (Gene Name=sidA)

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