Structure of PDB 4nsn Chain A

Receptor sequence
>4nsnA (length=273) Species: 431947 (Porphyromonas gingivalis ATCC 33277) [Search protein sequence]
MKLQEQHYHEAASFLSSRLPGDAKTAIILGSGLGELAEKIENKTVIPYNE
IPHFAQATAVGHKGNIIGGILGGTPVVAMQGRFHYYEGYSMDQVTFPIRV
MKLLGIENLFVSNAAGGINTSFKVGDLMIICDHINNLPNPLIGPNMDMFG
VRFPDMTRAYDREFIAKAKGIAQELNIPVKEGVYVGLTGPSYETPAEYKF
WGQVGGDAIGMSTVPEVIVARHTGIRVFGMSVITNEGYHFADDFVNDEQD
VIRAANAASEKMGAIFARLIAAV
3D structure
PDB4nsn Crystal structure of purine nucleoside phosphorylase from Porphyromonas gingivalis ATCC 33277, NYSGRC Target 030972, orthorhombic symmetry.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S46 H77 H99 Y101 E102 A129 M226 S227 N250 E263
Catalytic site (residue number reindexed from 1) S31 H62 H84 Y86 E87 A114 M211 S212 N235 E248
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 A129 A130 G131 Y207 E208 Y213 G225 M226 T249 N250 A114 A115 G116 Y192 E193 Y198 G210 M211 T234 N235
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4nsn, PDBe:4nsn, PDBj:4nsn
PDBsum4nsn
PubMed
UniProtB2RKN6

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