Structure of PDB 3nne Chain D

Receptor sequence
>3nneD (length=530) Species: 1665 (Arthrobacter globiformis) [Search protein sequence]
MHIDNIENLSDREFDYIVVGGGSAGAAVAARLSEDPAVSVALVEAGPDDR
GVPEVLQLDRWMELLESGYDWDYPIEPQENGNSFMRHARAKVMGGCSSHN
ACIAFWAPREDLDEWEAKYGATGWNAEAAWPLYKRLETNEDAGPDAPHHG
DSGPVHLMNVPPKDPTGVALLDACEQAGIPRAKFNTGTTVVNGANFFQIN
RRADGTRSSSSVSYIHPIVEQENFTLLTGLRARQLVFDADRRCTGVDIVD
SAFGHTHRLTARNEVVLSTGAIDTPKLLMLSGIGPAAHLAEHGIEVLVDS
PGVGEHLQDHPEGVVQFEAKQPMVAESTQWWEIGIFTPTEDGLDRPDLMM
HYGSVPFDMNTLRHGYPTTENGFSLTPNVTHARSRGTVRLRSRDFRDKPM
VDPRYFTDPEGHDMRVMVAGIRKAREIAAQPAMAEWTGRELSPGVEAQTD
EELQDYIRKTHNTVYHPVGTVRMGAVEDEMSPLDPELRVKGVTGLRVADA
SVMPEHVTVNPNITVMMIGERCADLIRSAR
3D structure
PDB3nne Structural and kinetic studies on the Ser101Ala variant of choline oxidase: Catalysis by compromise.
ChainD
Resolution2.47 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) I333 P377 N378 V464 H466 V509 N510
Catalytic site (residue number reindexed from 1) I333 P377 N378 V464 H466 V509 N510
Enzyme Commision number 1.1.3.17: choline 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 FAD D G22 S23 E44 A45 W71 R89 A90 G95 C96 H99 N100 A101 I103 A232 T269 D273 Y465 H466 D499 A500 N510 P511 N512 V515 G22 S23 E44 A45 W71 R89 A90 G95 C96 H99 N100 A101 I103 A232 T269 D273 Y465 H466 D499 A500 N510 P511 N512 V515
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0033713 choline:oxygen 1-oxidoreductase activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0019285 glycine betaine biosynthetic process from choline

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3nne, PDBe:3nne, PDBj:3nne
PDBsum3nne
PubMed20561507
UniProtQ7X2H8|CHOX_ARTGO Choline oxidase (Gene Name=codA)

[Back to BioLiP]