Structure of PDB 4ns1 Chain D

Receptor sequence
>4ns1D (length=270) Species: 431947 (Porphyromonas gingivalis ATCC 33277) [Search protein sequence]
FQSMKLQEQHYHEAASFLSSRLPGDAKTAIILGSGLGELAEKIENKTVIP
YNEIPHFAQKGNIIGGILGGTPVVAMQGRFHYYEGYSMDQVTFPIRVMKL
LGIENLFVSNAAGGINTSFKVGDLMIICDHINNLPNPLIGPNMDMFGVRF
PDMTRAYDREFIAKAKGIAQELNIPVKEGVYVGLTGPSYETPAEYKFWGQ
VGGDAIGMSTVPEVIVARHTGIRVFGMSVITNEGYHFADDFVNDEQDVIR
AANAASEKMGAIFARLIAAV
3D structure
PDB4ns1 Crystal structure of purine nucleoside phosphorylase from Porphyromonas gingivalis ATCC 33277, NYSGRC Target 30972.
ChainD
Resolution1.64 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 H99 Y101 E102 A129 M226 S227 N250 E263
Catalytic site (residue number reindexed from 1) S34 H81 Y83 E84 A111 M208 S209 N232 E245
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 DA D A129 A130 G131 E208 Y213 I224 G225 M226 T249 N250 A111 A112 G113 E190 Y195 I206 G207 M208 T231 N232
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:4ns1, PDBe:4ns1, PDBj:4ns1
PDBsum4ns1
PubMed
UniProtB2RKN6

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