Structure of PDB 4glj Chain A

Receptor sequence
>4gljA (length=287) Species: 77133 (uncultured bacterium) [Search protein sequence]
KNAADIAIIGGSGLYQMQALTNKRSVKIETPYGEPSDDIVLGELNGVTVA
FLTRHGQGHRLTPSEVPYRANIYALKTLGVRYIVSVSAVGSLQETLKPLD
MVIPDQMIDMTKQRVSTFFGDGAVAHVSMADPLCPEVADILIRAYDNADI
ADGQCHAKATYVCIEGPQFSTRAESHWYRQMQADIIGMTNMPEAKLAREA
SIAYATLALVTDFDCWHPNEQAVSADYAIQNLMKNADNAQQVIKQAVALI
ASEQPKSIAHTALTQALVTPVEAMSAETKTRLAALLP
3D structure
PDB4glj A study on the interaction of rhodamine B with methylthioadenosine phosphorylase protein sourced from an antarctic soil metagenomic library.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D222 D224
Catalytic site (residue number reindexed from 1) D212 D214
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 RHB A S22 Y25 H65 F179 I239 L242 S12 Y15 H55 F169 I229 L232
BS02 RHB A A98 G100 F179 I196 G197 M198 D222 F223 D224 N229 A238 A88 G90 F169 I186 G187 M188 D212 F213 D214 N219 A228
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:4glj, PDBe:4glj, PDBj:4glj
PDBsum4glj
PubMed23383268
UniProtC6KFA4

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