Structure of PDB 2a8y Chain F

Receptor sequence
>2a8yF (length=263) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MIEQNEKASIGIIGGSGLYDPGIFSESKEIKVYTPYGQPSDFITIGKIGN
KSVAFLPRHGRGHRIPPHKINYRANIWALKELGVRWVISVSAVGSLRMDY
KLGDFVIPDQFIDMTKNREYSFFDGPVVAHVSMADPFCNSLRKLAIETAK
ELNIKTHESGTYICIEGPRFSTRAESRTWREVYKADIIGMTLVPEVNLAC
EAQMCYATIAMVTDYDVFAEIPVTAEEVTRVMAENTEKAKKLLYALIQKL
PEKPCNSLKTALV
3D structure
PDB2a8y The crystal structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II from Sulfolobus solfataricus, a thermophilic enzyme stabilized by intramolecular disulfide bonds.
ChainF
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S16 P39 H63 I65 P66 A92 M190 T191 D214 D216 A225
Catalytic site (residue number reindexed from 1) S16 P39 H63 I65 P66 A92 M190 T191 D214 D216 A225
Enzyme Commision number 2.4.2.28: S-methyl-5'-thioadenosine phosphorylase.
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 MTA F V93 G94 F170 I188 M190 D214 A225 V228 V93 G94 F170 I188 M190 D214 A225 V228
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0017061 S-methyl-5-thioadenosine phosphorylase activity
Biological Process
GO:0006166 purine ribonucleoside salvage
GO:0009116 nucleoside metabolic process
GO:0019509 L-methionine salvage from methylthioadenosine
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2a8y, PDBe:2a8y, PDBj:2a8y
PDBsum2a8y
PubMed16414070
UniProtQ97W94|MTAP_SACS2 S-methyl-5'-thioadenosine phosphorylase (Gene Name=mtnP)

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