Structure of PDB 1brw Chain A

Receptor sequence

>1brwA (length=433) Species: 1422 (Geobacillus stearothermophilus)

MRMVDLIAKKRDGKALTKEEIEWIVRGYTNGDIPDYQMSALAMAIYFRGM
TEEETAALTMAMVQSGEMLDLSSIRGVKVDKHSTGGVGDTTTLVLGPLVA
SVGVPVAKMSGRGLGHTGGTIDKLESVPGFHVEISKDEFIRLVNENGIAI
IGQTGDLTPADKKLYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDV
KTGAGAFMKKLDEARRLARVMVDIGKRVGRRTMAVISDMSQPLGYAVGNA
LEVKEAIETLKGNGPHDLTELCLTLGSHMVYLAEKAPSLDEARRLLEEAI
RSGAAIAAFKTFLAAQGGDASVVDDLDKLPKAAYTSTVTAAADGYVAEMA
ADDIGTAAMWLGAGRAKKEDVIDLAVGIVLHKKIGDRVQKGEALATIHSN
RPDVLDVKEKIEAAIRLSPQPVARPPLIYETIV

3D structure

• PDB: 1brw The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation.
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H82 D161 R168 S183 K187
• Catalytic site (residue number reindexed from 1): H82 D161 R168 S183 K187
• Enzyme Commision number: 2.4.2.2: pyrimidine-nucleoside 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	PO4	A	K81 H82 S83 T92 K108	K81 H82 S83 T92 K108
BS02	CA	A	G88 T90 L243 A246 E255	G88 T90 L243 A246 E255

Gene Ontology

Molecular Function

• GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
• GO:0004850 uridine phosphorylase activity
• GO:0009032 thymidine phosphorylase activity
• GO:0016154 pyrimidine-nucleoside phosphorylase activity
• GO:0016757 glycosyltransferase activity
• GO:0016763 pentosyltransferase activity
• GO:0046872 metal ion binding
• GO:0047847 deoxyuridine phosphorylase activity

Biological Process

• GO:0006206 pyrimidine nucleobase metabolic process
• GO:0006213 pyrimidine nucleoside metabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1brw, PDBe:1brw, PDBj:1brw
• PDBsum: 1brw
• PubMed: 9817849
• UniProt: P77836|PDP_GEOSE Pyrimidine-nucleoside phosphorylase (Gene Name=pdp)