Structure of PDB 4m1e Chain F

Receptor sequence
>4m1eF (length=272) Species: 521674 (Planctopirus limnophila DSM 3776) [Search protein sequence]
ELKSRIDQATAKISQLWQGEPAVGMILGTGLGGLAEQIEQDIAIPYSDIP
HFPTSTVKSHAGRLVCGRLRGIPIVAMEGRFHYYEGYSLEQVTFPVRVMK
AMGVKTLLVTNAAGGINPQLDLSDVLIIEDHINLMPENPLRGPNDEELGP
RFPDMSHPYDCQHMEVARQVALELGIHCPKGVFVAVSGPNLETRAEYRML
KLMGADVVGMSTVPEVLVAVHAGLRVLGFSVVTDLCLPDALEPVELNKIL
EVAARGGAKLARLIPEILPRIA
3D structure
PDB4m1e Crystal structure of purine nucleoside phosphorylase I from Planctomyces limnophilus DSM 3776, NYSGRC Target 029364.
ChainF
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) 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 6PC F Q121 H179 P181 Q119 H177 P179
BS02 ADE F A114 A115 G116 L193 E194 V210 M212 D236 A112 A113 G114 L191 E192 V208 M210 D234
BS03 6PC F R170 K182 R168 K180
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

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Cellular Component
External links
PDB RCSB:4m1e, PDBe:4m1e, PDBj:4m1e
PDBsum4m1e
PubMed
UniProtD5SMY7

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