Structure of PDB 2wpf Chain D

Receptor sequence

>2wpfD (length=491) Species: 185431 (Trypanosoma brucei brucei TREU927) [Search protein sequence]

GSHMSKAFDLVVIGAGSGGLEAGWNAATLYGKRVAVVDVQTSHGPPFYAA
LGGTCVNVGCVPKKLMVTGAQYMDHLRESAGFGWEFDGSSVKANWKKLIA
AKNEAVLDINKSYEGMFNDTEGLDFFLGWGSLESKNVVVVRETADPKSAV
KERLQADHILLATGSWPQMPAIPGIEHCISSNEAFYLPEPPRRVLTVGGG
FISVEFAGIFNAYKPPGGKVTLCYRNNLILRGFDETIREEVTKQLTANGI
EIMTNENPAKVSLNTDGSKHVTFESGKTLDVDVVMMAIGRIPRTNDLQLG
NVGVKLTPKGGVQVDEFSRTNVPNIYAIGDITDRLMLTPVAINEGAALVD
TVFGNKPRKTDHTRVASAVFSIPPIGTCGLIEEVAAKEFEKVAVYMSSFT
PLMHNISGSKYKKFVAKIVTNHSDGTVLGVHLLGDGAPEIIQAVGVCLRL
NAKISDFYNTIGVHPTSAEELCSMRTPSYYYVKGEKMEKLP

3D structure

PDB

2wpf Dihydroquinazolines as a Novel Class of Trypanosoma Brucei Trypanothione Reductase Inhibitors: Discovery, Synthesis, and Characterization of Their Binding Mode by Protein Crystallography.

Chain

Resolution

1.9 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	S14 L48 C52 C57 K60 G85 S86 F198 E202 I339 G459 H461 E466 E485 K486
Catalytic site (residue number reindexed from 1)	S17 L51 C55 C60 K63 G88 S89 F201 E205 I342 G462 H464 E469 E488 K489
Enzyme Commision number	1.8.1.12: trypanothione-disulfide reductase.

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	I10 G11 G13 S14 G15 V34 D35 V36 A46 A47 G50 T51 C52 G56 C57 K60 G127 T160 G161 F198 I199 R287 R290 G326 D327 M333 L334 T335 A338	I13 G14 G16 S17 G18 V37 D38 V39 A49 A50 G53 T54 C55 G59 C60 K63 G130 T163 G164 F201 I202 R290 R293 G329 D330 M336 L337 T338 A341
BS02	WPF	D	S14 L17 E18 W21 Y110 M113 F114	S17 L20 E21 W24 Y113 M116 F117	MOAD: ic50=0.23uM

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0004791	thioredoxin-disulfide reductase (NADPH) activity
GO:0015036	disulfide oxidoreductase activity
GO:0015042	trypanothione-disulfide reductase (NADPH) activity
GO:0016491	oxidoreductase activity
GO:0016668	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0046872	metal ion binding
GO:0050660	flavin adenine dinucleotide binding

	Biological Process
GO:0045454	cell redox homeostasis
GO:0098869	cellular oxidant detoxification

	Cellular Component
GO:0005654	nucleoplasm
GO:0005737	cytoplasm
GO:0020015	glycosome
GO:0097014	ciliary plasm

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:2wpf, PDBe:2wpf, PDBj:2wpf
PDBsum	2wpf
PubMed	21851087
UniProt	Q389T8

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