Structure of PDB 7ljt Chain C

Receptor sequence

>7ljtC (length=1015) Species: 9823 (Sus scrofa) [Search protein sequence]

PVLSKDVADIESILALNPRTQSHAALHSTLAKKLDKKHWKRNPDKNCFHC
EKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTHLDIKSFIT
SISNKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGSINI
GGLQQFASEVFKAMNIPQIRNPCLPSQEKMPEAYSAKIALLGAGPASISC
ASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLG
VKIICGKSLSENEITLNTLKEEGYKAAFIGIGLPEPKTDDIFQGLTQDQG
FYTSKDFLPLVAKSSKAGMCACHSPLPSIRGAVIVLGAGDTAFDCATSAL
RCGARRVFLVFRKGFVNIRAVPEEVELAKEEKCEFLPFLSPRKVIVKGGR
IVAVQFVRTEQDETGKWNEDEDQIVHLKADVVISAFGSVLRDPKVKEALS
PIKFNRWDLPEVDPETMQTSEPWVFAGGDIVGMANTTVESVNDGKQASWY
IHKYIQAQYGASVSAKPELPLFYTPVDLVDISVEMAGLKFINPFGLASAA
PTTSSSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIVRGTTSGPMYGP
GQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWME
LSRKAEASGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAV
QIPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLMGLKADGTPWP
AVGAGKRTTYGGVSGTAIRPIALRAVTTIARALPGFPILATGGIDSAESG
LQFLHSGASVLQVCSAVQNQDFTVIQDYCTGLKALLYLKSIEELQGWDGQ
SPGTESHQKGKPVPRIAELMGKKLPNFGPYLEQRKKIIAEEKMRLKEQNA
AFPPLERKPFIPKKPIPAIKDVIGKALQYLGTFGELSNIEQVVAVIDEEM
CINCGKCYMTCNDSGYQAIQFDPETHLPTVTDTCTGCTLCLSVCPIIDCI
RMVSRTTPYEPKRGL

3D structure

PDB

7ljt The Interaction of Porcine Dihydropyrimidine Dehydrogenase with the Chemotherapy Sensitizer: 5-Ethynyluracil.

Chain

Resolution

1.98 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	K574 C671 K709
Catalytic site (residue number reindexed from 1)	K572 C669 K707
Enzyme Commision number	1.3.1.2: dihydropyrimidine dehydrogenase (NADP(+)).

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	SF4	C	C953 I954 N955 C956 G957 C959 P980 C996 P997 C1001 I1002	C951 I952 N953 C954 G955 C957 P978 C994 P995 C999 I1000
BS02	SF4	C	C963 Y968 I971 C986 T987 G988 C989 T990 C992	C961 Y966 I969 C984 T985 G986 C987 T988 C990
BS03	SF4	C	C79 L80 K81 C82 P86 C87 C140 N141 L142 I150 I152	C77 L78 K79 C80 P84 C85 C138 N139 L140 I148 I150
BS04	SF4	C	C91 L95 I97 C130 L135 C136 Q156	C89 L93 I95 C128 L133 C134 Q154
BS05	FAD	C	V129 G194 G196 P197 A198 E218 K219 G225 L226 E230 I231 R235 S260 L261 I283 G284 G480 D481 T488 T489 S492	V127 G192 G194 P195 A196 E216 K217 G223 L224 E228 I229 R233 S258 L259 I281 G282 G478 D479 T486 T487 S490
BS06	FMN	C	S550 A551 K574 T575 N609 N668 K709 N736 T737 S766 G767 T793 G794 G795 C816 S817 Q820	S548 A549 K572 T573 N607 N666 K707 N734 T735 S764 G765 T791 G792 G793 C814 S815 Q818
BS07	Y3G	C	N609 E611 I613 N668 C671 H673 N736 T737	N607 E609 I611 N666 C669 H671 N734 T735
BS08	NAP	C	P131 G339 A340 G341 D342 T343 R364 K365 R371 E376 A437 F438 G439 N487	P129 G337 A338 G339 D340 T341 R362 K363 R369 E374 A435 F436 G437 N485

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0002058	uracil binding
GO:0010181	FMN binding
GO:0016491	oxidoreductase activity
GO:0016627	oxidoreductase activity, acting on the CH-CH group of donors
GO:0017113	dihydropyrimidine dehydrogenase (NADP+) activity
GO:0042803	protein homodimerization activity
GO:0046872	metal ion binding
GO:0050660	flavin adenine dinucleotide binding
GO:0050661	NADP binding
GO:0051536	iron-sulfur cluster binding
GO:0051539	4 iron, 4 sulfur cluster binding

	Biological Process
GO:0006210	thymine catabolic process
GO:0006212	uracil catabolic process
GO:0006214	thymidine catabolic process
GO:0019483	beta-alanine biosynthetic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:7ljt, PDBe:7ljt, PDBj:7ljt
PDBsum	7ljt
PubMed	33755421
UniProt	Q28943\|DPYD_PIG Dihydropyrimidine dehydrogenase [NADP(+)] (Gene Name=DPYD)

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