Structure of PDB 1jrp Chain D

Receptor sequence
>1jrpD (length=760) Species: 1061 (Rhodobacter capsulatus) [Search protein sequence]
SVGKPLPHDSARAHVTGQARYLDDLPCPANTLHLAFGLSTEASAAITGLD
LEPVRESPGVIAVFTAADLPHDNDASPAPSPEPVLATGEVHFVGQPIFLV
AATSHRAARIAARKARITYAPRPAILTLDQALAADSRFEGGPVIWARGDV
ETALAGAAHLAEGCFEIGGQEHFYLEGQAALALPAEGGVVIHCSSQHPSE
IQHKVAHALGLAFHDVRVEMRRMGGGFGGKESQGNHLAIACAVAARATGR
PCKMRYDRDDDMVITGKRHDFRIRYRIGADASGKLLGADFVHLARCGWSA
DLSLPVCDRAMLHADGSYFVPALRIESHRLRTNTQSNTAFRGFGGPQGAL
GMERAIEHLARGMGRDPAELRALNFYDPPEKKTQTTHYGQEVADCVLGEL
VTRLQKSANFTTRRAEIAAWNSTNRTLARGIALSPVKFGISFTLTHLNQA
GALVQIYTDGSVALNHGGTEMGQGLHAKMVQVAAAVLGIDPVQVRITATD
TSKVPNTSATAASSGADMNGMAVKDACETLRGRLAGFVAAREGCAARDVI
FDAGQVQASGKSWRFAEIVAAAYMARISLSATGFYATPKLSWDRLRGQGR
PFLYFAYGAAITEVVIDRLTGENRILRTDILHDAGASLNPALDIGQIEGA
YVQGAGWLTTEELVWDHCGRLMTHAPSTYKIPAFSDRPRIFNVALWDQPN
REETIFRSKAVGEPPFLLGISAFLALHDACAACGPHWPDLQAPATPEAVL
AAVRRAEGRA
3D structure
PDB1jrp Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus
ChainD
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q197 E232 R310 H314 R342 G729 E730
Catalytic site (residue number reindexed from 1) Q196 E231 R309 H313 R341 G712 E713
Enzyme Commision number 1.1.1.204: Transferred entry: 1.17.1.4.
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 CA D E172 H173 Y175 T266 G267 E171 H172 Y174 T265 G266
BS02 141 D E232 R310 F344 F459 A528 A529 E730 E231 R309 F343 F442 A511 A512 E713
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0030151 molybdenum ion binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:1jrp, PDBe:1jrp, PDBj:1jrp
PDBsum1jrp
PubMed11796116
UniProtO54051

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