Structure of PDB 1n1p Chain A

Receptor sequence
>1n1pA (length=498) Species: 1931 (Streptomyces sp.) [Search protein sequence]
GYVPAVVIGTGYGAAVSALRLGEAGVQTLMLEMGQLWNQPGPDGNIFCGM
LNPDKRSSWFKNRTEAPLGSFLWLDVVNRNIDPYAGVLDRVNYDQMSVYV
GRGVGGGSLVNGGMAVEPKRSYFEEILPRVDSSEMYDRYFPRANSMLRVN
HIDTKWFEDTEWYKFARVSREQAGKAGLGTVFVPNVYDFGYMQREAAGEV
PKSALATEVIYGNNHGKQSLDKTYLAAALGTGKVTIQTLHQVKTIRQTKD
GGYALTVEQKDTDGKLLATKEISCRYLFLGAGSLGSTELLVRARDTGTLP
NLNSEVGAGWGPNGNIMTARANHMWNPTGAHQSSIPALGIDAWDNSDSSV
FAEIAPMPAGLETWVSLYLAITKNPQRGTFVYDAATDRAKLNWTRDQNAP
AVNAAKALFDRINKANGTIYRYDLFGTQLKAFADDFCYHPLGGCVLGKAT
DDYGRVAGYKNLYVTDGSLIPGSVGVNPFVTITALAERNVERIIKQDV
3D structure
PDB1n1p Atomic Resolution Density Maps Reveal Secondary Structure Dependent Differences in Electronic Distribution
ChainA
Resolution0.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E361 H447 N485
Catalytic site (residue number reindexed from 1) E353 H439 N477
Enzyme Commision number 1.1.3.6: cholesterol oxidase.
5.3.3.1: steroid Delta-isomerase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004769 steroid delta-isomerase activity
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0016853 isomerase activity
GO:0016995 cholesterol oxidase activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0006707 cholesterol catabolic process
GO:0008203 cholesterol metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1n1p, PDBe:1n1p, PDBj:1n1p
PDBsum1n1p
PubMed14558826
UniProtP12676|CHOD_STRS0 Cholesterol oxidase (Gene Name=choA)

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