Structure of PDB 3t8i Chain D

Receptor sequence
>3t8iD (length=306) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence]
MRKVIVDSDTATDDTIAILLASRFFQLLGVTIVAGNVNYNQEVKNALFTL
EYIGKQDVPVYLGSQRPILGNWRTVEEVHGSNGMSNWNYPEPNKRPEKEH
AIDAILRLSKEHEGELEILAISPLTNIALAYLKDPSVVKRVKKIWIMGGA
FSKGNTTPIAEFNFWVDPEAAKIVLDAGFDITIVPWEVAEISGSLNERDW
EYISKLNTKLSNFFINVNKTLKEYTTKNQGISGSIHPDSLTVSIAHDNSI
ILDSSLKYVDVELCSKSRGAMLIDWYSLHKNKPNAEIVLKADGGKFKNLL
FNSLSQ
3D structure
PDB3t8i New Determinants in the Catalytic Mechanism of Nucleoside Hydrolases from the Structures of Two Isozymes from Sulfolobus solfataricus.
ChainD
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D9 D14 N36 I121 F162 N163 P237 D238
Catalytic site (residue number reindexed from 1) D9 D14 N36 I121 F162 N163 P237 D238
Enzyme Commision number 3.2.2.1: purine nucleosidase.
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 D9 D14 I121 D238 D9 D14 I121 D238
Gene Ontology
Molecular Function
GO:0008477 purine nucleosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0046872 metal ion binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006152 purine nucleoside catabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3t8i, PDBe:3t8i, PDBj:3t8i
PDBsum3t8i
PubMed22551416
UniProtQ97WH6

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