Structure of PDB 4yrw Chain A
Receptor sequence
>4yrwA (length=1289) Species:
10116
(Rattus norvegicus) [
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ADELVFFVNGKKVVEKNADPETTLLVYLRRKLGLCGTKLGCGEGGCGACT
VMISKYDRLQNKIVHFSVNACLAPICSLHHVAVTTVEGIGNTQKLHPVQE
RIARSHGSQCGFCTPGIVMSMYTLLRNQPEPTVEEIENAFQGNLCRCTGY
RPILQGFRTFAKDLSPSLFNPEDFKPLDPTQEPIFPPELLRLKDTPQKKL
RFEGERVTWIQASTMEELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPL
IVCPAWIPELNSVVHGPEGISFGASCPLSLVESVLAEEIAKLPEQKTEVF
RGVMEQLRWFAGKQVKSVASIGGNIITASPISDLNPVFMASGAKLTLVSR
GTRRTVRMDHTFFPGYRKTLLRPEEILLSIEIPYSKEGEFFSAFKQASRR
EDDIAKVTSGMRVLFKPGTIEVQELSLCFGGMADRTISALKTTPKQLSKS
WNEELLQSVCAGLAEELQLAPDAPGGMVEFRRTLTLSFFFKFYLTVLQKL
GRADLEDMCGKLDPTFASATLLFQKDPPANVQLFQEVPKDQSEEDMVGRP
LPHLAANMQASGEAVYCDDIPRYENELSLRLVTSTRAHAKITSIDTSEAK
KVPGFVCFLTAEDVPNSNATGLFNDETVFAKDEVTCVGHIIGAVVADTPE
HAQRAARGVKITYEDLPAIITIQDAINNNSFYGSEIKIEKGDLKKGFSEA
DNVVSGELYIGGQEHFYLETNCTIAVPKGEAGEMELFVSTQNTMKTQSFV
AKMLGVPDNRIVVRVKRMGGGFGGKETRSTVVSTALALAAHKTGRPVRCM
LDRDEDMLITGGRHPFLAKYKVGFMKTGTVVALEVAHFSNGGNTEDLSRS
IMERALFHMDNAYKIPNIRGTGRICKTNLPSNTAFRGFGGPQGMLIAEYW
MSEVAITCGLPAEEVRRKNMYKEGDLTHFNQKLEGFTLPRCWDECIASSQ
YLARKREVEKFNRENCWKKRGLCIIPTKFGISFTLPFLNQGGALVHVYTD
GSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIHISETSTNTVPNTSP
TAASASADLNGQGVYEACQTILKRLEPFKKKKPTGPWEAWVMDAYTSAVS
LSATGFYKTPNLGYSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRT
DIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTMEELHYSPEGSLHTRGPST
YKIPAFGSIPIEFRVSLLRDCPNKRAIYASKAVGEPPLFLASSIFFAIKD
AIRAARAQHGDNAKQLFQLDSPATPEKIRNACVDQFTTL
3D structure
PDB
4yrw
The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase
Chain
A
Resolution
1.99 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
Q767 E802 R880 H884 R912 G1260 E1261
Catalytic site (residue number reindexed from 1)
Q741 E776 R854 H858 R886 G1234 E1235
Enzyme Commision number
1.17.1.4
: xanthine dehydrogenase.
1.17.3.2
: xanthine 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
FES
A
Q111 C112 G113 C115 C147 C149 L744
Q109 C110 G111 C113 C145 C147 L718
BS02
FES
A
G42 C43 G44 G46 C48 G49 C51 C73
G40 C41 G42 G44 C46 G47 C49 C71
BS03
BCT
A
R839 H840 I877 A910 F914 G915 Q918
R813 H814 I851 A884 F888 G889 Q892
BS04
CA
A
G867 T870 E871 S874 S907 N908
G841 T844 E845 S848 S881 N882
BS05
FAD
A
G46 K255 L256 V257 V258 G259 N260 T261 E262 I263 F336 A337 A345 S346 G349 N350 I352 T353 S358 D359 I402 L403
G44 K229 L230 V231 V232 G233 N234 T235 E236 I237 F310 A311 A319 S320 G323 N324 I326 T327 S332 D333 I376 L377
BS06
URC
A
E802 R880 F914 F1009 T1010 A1079 E1261
E776 R854 F888 F983 T984 A1053 E1235
Gene Ontology
Molecular Function
GO:0004854
xanthine dehydrogenase activity
GO:0004855
xanthine oxidase activity
GO:0005506
iron ion binding
GO:0016491
oxidoreductase activity
GO:0042802
identical protein binding
GO:0042803
protein homodimerization activity
GO:0043546
molybdopterin cofactor binding
GO:0046872
metal ion binding
GO:0050421
nitrite reductase (NO-forming) activity
GO:0050660
flavin adenine dinucleotide binding
GO:0051536
iron-sulfur cluster binding
GO:0051537
2 iron, 2 sulfur cluster binding
GO:0070674
hypoxanthine dehydrogenase activity
GO:0070675
hypoxanthine oxidase activity
GO:0071949
FAD binding
Biological Process
GO:0000255
allantoin metabolic process
GO:0001937
negative regulation of endothelial cell proliferation
GO:0006147
guanine catabolic process
GO:0006148
inosine catabolic process
GO:0006149
deoxyinosine catabolic process
GO:0006154
adenosine catabolic process
GO:0006157
deoxyadenosine catabolic process
GO:0006161
deoxyguanosine catabolic process
GO:0006196
AMP catabolic process
GO:0006204
IMP catabolic process
GO:0007595
lactation
GO:0009114
hypoxanthine catabolic process
GO:0009115
xanthine catabolic process
GO:0010044
response to aluminum ion
GO:0010629
negative regulation of gene expression
GO:0016226
iron-sulfur cluster assembly
GO:0030856
regulation of epithelial cell differentiation
GO:0032496
response to lipopolysaccharide
GO:0034465
response to carbon monoxide
GO:0042542
response to hydrogen peroxide
GO:0043605
amide catabolic process
GO:0045602
negative regulation of endothelial cell differentiation
GO:0046038
GMP catabolic process
GO:0046055
dGMP catabolic process
GO:0046059
dAMP catabolic process
GO:0051898
negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
GO:0071347
cellular response to interleukin-1
GO:0071356
cellular response to tumor necrosis factor
GO:0097184
response to azide
GO:1900745
positive regulation of p38MAPK cascade
GO:1900747
negative regulation of vascular endothelial growth factor signaling pathway
GO:2000379
positive regulation of reactive oxygen species metabolic process
GO:2001213
negative regulation of vasculogenesis
Cellular Component
GO:0005576
extracellular region
GO:0005615
extracellular space
GO:0005737
cytoplasm
GO:0005777
peroxisome
GO:0005829
cytosol
GO:0016529
sarcoplasmic reticulum
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:4yrw
,
PDBe:4yrw
,
PDBj:4yrw
PDBsum
4yrw
PubMed
25817260
UniProt
P22985
|XDH_RAT Xanthine dehydrogenase/oxidase (Gene Name=Xdh)
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