Structure of PDB 2w55 Chain B

Receptor sequence
>2w55B (length=760) Species: 1061 (Rhodobacter capsulatus) [Search protein sequence]
SVGKPLPHDSARAHVTGQARYLDDLPCPANTLHLAFGLSTEASAAITGLD
LEPVRESPGVIAVFTAADLPHDNDASPAPSPEPVLATGEVHFVGQPIFLV
AATSHRAARIAARKARITYAPRPAILTLDQALAADSRFEGGPVIWARGDV
ETALAGAAHLAEGCFEIGGQEHFYLEGQAALALPAEGGVVIHCSSQHPSE
IQHKVAHALGLAFHDVRVEMRRMGGGFGGKQSQGNHLAIACAVAARATGR
PCKMRYDRDDDMVITGKRHDFRIRYRIGADASGKLLGADFVHLARCGWSA
DLSLPVCDRAMLHADGSYFVPALRIESHRLRTNTQSNTAFRGFGGPQGAL
GMERAIEHLARGMGRDPAELRALNFYDPPEKKTQTTHYGQEVADCVLGEL
VTRLQKSANFTTRRAEIAAWNSTNRTLARGIALSPVKFGISFTLTHLNQA
GALVQIYTDGSVALNHGGTEMGQGLHAKMVQVAAAVLGIDPVQVRITATD
TSKVPNTSATAASSGADMNGMAVKDACETLRGRLAGFVAAREGCAARDVI
FDAGQVQASGKSWRFAEIVAAAYMARISLSATGFYATPKLSWDRLRGQGR
PFLYFAYGAAITEVVIDRLTGENRILRTDILHDAGASLNPALDIGQIEGA
YVQGAGWLTTEELVWDHCGRLMTHAPSTYKIPAFSDRPRIFNVALWDQPN
REETIFRSKAVGEPPFLLGISAFLALHDACAACGPHWPDLQAPATPEAVL
AAVRRAEGRA
3D structure
PDB2w55 Mechanism of Substrate and Inhibitor Binding of Rhodobacter Capsulatus Xanthine Dehydrogenase.
ChainB
Resolution3.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Q197 Q232 R310 H314 R342 G729 E730
Catalytic site (residue number reindexed from 1) Q196 Q231 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 XAX B G226 G227 F228 G229 Q232 F341 R342 M488 G489 Q490 A528 A529 S530 G532 Q663 E730 G225 G226 F227 G228 Q231 F340 R341 M471 G472 Q473 A511 A512 S513 G515 Q646 E713
BS02 HPA B Q232 R310 F344 F459 T460 A529 Q231 R309 F343 F442 T443 A512
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:2w55, PDBe:2w55, PDBj:2w55
PDBsum2w55
PubMed19109249
UniProtO54051

[Back to BioLiP]