Structure of PDB 2uzz Chain A

Receptor sequence
>2uzzA (length=371) Species: 469008 (Escherichia coli BL21(DE3)) [Search protein sequence]
KYDLIIIGSGSVGAAAGYYATRAGLNVLMTDAHMPPHQHGSHHGDTRLIR
HAYGEGEKYVPLVLRAQMLWDELSRHNEDDPIFVRSGVINLGPADSTFLA
NVAHSAEQWQLNVEKLDAQGIMARWPEIRVPDNYIGLFETDSGFLRSELA
IKTWIQLAKEAGCAQLFNCPVTAIRHDDDGVTIETADGEYQAKKAIVCAG
TWVKDLLPELPVQPVRKVFAWYQADGRYSVKNKFPAFTGELPNGDQYYGF
PAENDALKIGKHNGGQVIHSADERVPFAEVVSDGSEAFPFLRNVLPGIGC
CLYGAACTYDNSPDEDFIIDTLPGHDNTLLITGLSGHGFKFASVLGEIAA
DFAQDKKSDFDLTPFRLSRFQ
3D structure
PDB2uzz The X-Ray Structure of N-Methyltryptophan Oxidase Reveals the Structural Determinants of Substrate Specificity.
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H44 T47 R48 R51 S97 Y249 K259 H263 C308 H338 K341
Catalytic site (residue number reindexed from 1) H43 T46 R47 R50 S96 Y248 K258 H262 C307 H337 K340
Enzyme Commision number 1.5.3.-
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 A G11 S12 V13 D32 A33 H38 G41 S42 H43 R48 L49 V172 A200 G201 F220 Y249 C308 T309 Y310 G337 G339 F340 K341 G10 S11 V12 D31 A32 H37 G40 S41 H42 R47 L48 V171 A199 G200 F219 Y248 C307 T308 Y309 G336 G338 F339 K340
Gene Ontology
Molecular Function
GO:0008115 sarcosine oxidase activity
GO:0016491 oxidoreductase activity
GO:0016647 oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor
GO:0050131 N-methyl-L-amino-acid oxidase activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0006974 DNA damage response
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2uzz, PDBe:2uzz, PDBj:2uzz
PDBsum2uzz
PubMed18186483
UniProtP40874|MTOX_ECOLI N-methyl-L-tryptophan oxidase (Gene Name=solA)

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