Structure of PDB 2i0k Chain A

Receptor sequence
>2i0kA (length=536) Species: 1702 (Brevibacterium sterolicum) [Search protein sequence]
APLPTPPNFPNDIALFQQAYQNWSKEIMLDATWVCSPKTPQDVVRLANWA
HEHDYKIRPRGAMAGWTPLTVEKGANVEKVILADTMTHLNGITVNTGGPV
ATVTAGAGASIEAIVTELQKHDLGWANLPAPGVLSIGGALAVNAHGAALP
AVGQTTLPGHTYGSLSNLVTELTAVVWNGTTYALETYQRNDPRITPLLTN
LGRCFLTSVTMQAGPNFRQRCQSYTDIPWRELFAPKGADGRTFEKFVAES
GGAEAIWYPFTEKPWMKVWTVSGKPPQAREVSGPYNYIFSDNLPEPITDM
IGAINAGNPGIAPLFGPAMYEITKLGLAATNANDIWGWSKDVQFYIKATT
LRLTEGGGAVVTSRANIATVINDFTEWFHERIEFYRAKGEFPLNGPVEIR
CCGLDQAADVKVPSVGPPTISATRPRPDHPDWDVAIWLNVLGVPGTPGMF
EFYREMEQWMRSHYNNDDATFRPEWSKGWAFGPDPYTDNDIVTNKMRATY
IEGVPTTENWDTARARYNQIDPHRVFTNGFMDKLLP
3D structure
PDB2i0k Structural and kinetic analyses of the H121A mutant of cholesterol oxidase.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A121 E311 E475 R477
Catalytic site (residue number reindexed from 1) A64 E254 E398 R400
Enzyme Commision number 1.1.3.6: cholesterol oxidase.
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 MN A N542 E579 N465 E502
BS02 MN A D544 D545 D467 D468
BS03 FAD A W80 P116 G118 A119 M120 A121 W123 A187 P188 S192 G195 A198 V199 A201 H202 L258 G259 L263 R477 S553 W23 P59 G61 A62 M63 A64 W66 A130 P131 S135 G138 A141 V142 A144 H145 L201 G202 L206 R400 S476
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0016491 oxidoreductase activity
GO:0016899 oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding

View graph for
Molecular Function
External links
PDB RCSB:2i0k, PDBe:2i0k, PDBj:2i0k
PDBsum2i0k
PubMed16856877
UniProtQ7SID9

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