Structure of PDB 6rtm Chain A

Receptor sequence

>6rtmA (length=587) Species: 6183 (Schistosoma mansoni) [Search protein sequence]

TSQWLRKTVDSAAVILFSKTTCPYCKKVKDVLAEAKIKHATIELDQLSNG
SAIQKCLASFSKIETVPQMFVRGKFIGDSQTVLKYYSNDELAGIVNESKY
DYDLIVIGGGSGGLAAGKEAAKYGAKTAVLDYVEPTPIGTTWGLGGTCVN
VGCIPKKLMHQAGLLSHALEDAEHFGWSLDRSKISHNWSTMVEGVQSHIG
SLNWGYKVALRDNQVTYLNAKGRLISPHEVQITDKNQKVSTITGNKIILA
TGERPKYPEIPGAVEYGITSDDLFSLPYFPGKTLVIGASYVALECAGFLA
SLGGDVTVMVRSILLRGFDQQMAEKVGDYMENHGVKFAKLCVPDEIKQLK
VVDTENNKPGLLLVKGHYTDGKKFEEEFETVIFAVGREPQLSKVLCETVG
VKLDKNGRVVCTDDEQTTVSNVYAIGDINAGKPQLTPVAIQAGRYLARRL
FAGATELTDYSNVATTVFTPLEYGACGLSEEDAIEKYGDKDIEVYHSNFK
PLEWTVAHREDNVCYMKLVCRKSDNMRVLGLHVLGPNAGEITQGYAVAIK
MGATKADFDRTIGIHPTCSETFTTLHVTKKSGVSPIV

3D structure

PDB

6rtm Ectopic suicide inhibition of thioredoxin glutathione reductase.

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	L150 C154 C159 K162 Y296 E300 G569 H571 E576
Catalytic site (residue number reindexed from 1)	L144 C148 C153 K156 Y290 E294 G563 H565 E570
Enzyme Commision number	1.8.1.9: thioredoxin-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	A	G114 D137 Y138 G152 T153 C154 G158 C159 K162 G228 T257 G258 Y296 V297 R393 G432 D433 Q440 L441 T442	G108 D131 Y132 G146 T147 C148 G152 C153 K156 G222 T251 G252 Y290 V291 R387 G426 D427 Q434 L435 T436
BS02	KJH	A	V316 L320 E330 D334 F343 K345	V310 L314 E324 D328 F337 K339

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0004362	glutathione-disulfide reductase (NADPH) activity
GO:0004791	thioredoxin-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:0006749	glutathione metabolic process
GO:0034599	cellular response to oxidative stress
GO:0045454	cell redox homeostasis
GO:0098869	cellular oxidant detoxification

	Cellular Component
GO:0005739	mitochondrion
GO:0005829	cytosol

View graph for
Molecular Function

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:6rtm, PDBe:6rtm, PDBj:6rtm
PDBsum	6rtm
PubMed	31870799
UniProt	A0A3Q0KFL1

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