Structure of PDB 4m1e Chain A

Receptor sequence

>4m1eA (length=272) Species: 521674 (Planctopirus limnophila DSM 3776)

ELKSRIDQATAKISQLWQGEPAVGMILGTGLGGLAEQIEQDIAIPYSDIP
HFPTSTVKSHAGRLVCGRLRGIPIVAMEGRFHYYEGYSLEQVTFPVRVMK
AMGVKTLLVTNAAGGINPQLDLSDVLIIEDHINLMPENPLRGPNDEELGP
RFPDMSHPYDCQHMEVARQVALELGIHCPKGVFVAVSGPNLETRAEYRML
KLMGADVVGMSTVPEVLVAVHAGLRVLGFSVVTDLCLPDALEPVELNKIL
EVAARGGAKLARLIPEILPRIA

3D structure

• PDB: 4m1e Crystal structure of purine nucleoside phosphorylase I from Planctomyces limnophilus DSM 3776, NYSGRC Target 029364.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T31 H62 H84 Y86 E87 A114 M212 S213 D236 C238 L248
• Catalytic site (residue number reindexed from 1): T29 H60 H82 Y84 E85 A112 M210 S211 D234 C236 L246
• 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	ADE	A	A114 A115 G116 L193 E194 V210 M212 D236	A112 A113 G114 L191 E192 V208 M210 D234
BS02	6PC	A	R170 P181 K182	R168 P179 K180
BS03	6PC	A	N119 Q121 L122 H179 P181	N117 Q119 L120 H177 P179

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004731 purine-nucleoside phosphorylase activity
• GO:0016757 glycosyltransferase activity
• GO:0016763 pentosyltransferase activity

Biological Process

• GO:0006139 nucleobase-containing compound metabolic process
• GO:0009116 nucleoside metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:4m1e, PDBe:4m1e, PDBj:4m1e
• PDBsum: 4m1e
• UniProt: D5SMY7