Structure of PDB 3opv Chain K

Receptor sequence

>3opvK (length=237) Species: 83333 (Escherichia coli K-12)

ATPHINAEMGDFADVVLMPGDPLAAKYIAETFLEDAREVNNVRGMLGFTG
TYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL
RDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARV
GNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK

3D structure

• PDB: 3opv Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.
• Chain: K
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H4 G20 A24 R43 E75 R87 S90 S203 D204 I206 R217
• Catalytic site (residue number reindexed from 1): H4 G20 A24 R43 E75 R87 S90 S203 D204 I206 R217
• Enzyme Commision number: 2.4.2.1: purine-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	K	G20 R87 S90	G20 R87 S90

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004731 purine-nucleoside phosphorylase activity
• GO:0016757 glycosyltransferase activity
• GO:0016763 pentosyltransferase activity
• GO:0042802 identical protein binding
• GO:0047975 guanosine phosphorylase activity

Biological Process

• GO:0006139 nucleobase-containing compound metabolic process
• GO:0006152 purine nucleoside catabolic process
• GO:0006974 DNA damage response
• GO:0009116 nucleoside metabolic process
• GO:0009164 nucleoside catabolic process
• GO:0019686 purine nucleoside interconversion
• GO:0042278 purine nucleoside metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0016020 membrane

External links

• PDB: RCSB:3opv, PDBe:3opv, PDBj:3opv
• PDBsum: 3opv
• PubMed: 21672603
• UniProt: P0ABP8|DEOD_ECOLI Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)