Structure of PDB 1rt9 Chain A
Receptor sequence
>1rt9A (length=282) Species:
9606
(Homo sapiens) [
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NGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYSE
IPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRV
FHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPND
ERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFET
VAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESL
EKANHEEVLAAGKQAAQKLEQFVSILMASIPL
3D structure
PDB
1rt9
Structural comparison of human and malarial purine nucleoside phosphorylases
Chain
A
Resolution
2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
S33 H64 H86 Y88 E89 A116 M219 S220 N243 V245 H257
Catalytic site (residue number reindexed from 1)
S31 H62 H84 Y86 E87 A114 M217 S218 N241 V243 H255
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
IMH
A
Y88 A116 A117 G118 F200 E201 V217 M219 N243 H257
Y86 A114 A115 G116 F198 E199 V215 M217 N241 H255
PDBbind-CN
: -logKd/Ki=10.25,Ki=56pM
Gene Ontology
Molecular Function
GO:0001882
nucleoside binding
GO:0002060
purine nucleobase binding
GO:0003824
catalytic activity
GO:0004731
purine-nucleoside phosphorylase activity
GO:0005515
protein binding
GO:0016757
glycosyltransferase activity
GO:0016763
pentosyltransferase activity
GO:0042301
phosphate ion binding
GO:0042802
identical protein binding
GO:0047975
guanosine phosphorylase activity
Biological Process
GO:0000255
allantoin metabolic process
GO:0006139
nucleobase-containing compound metabolic process
GO:0006148
inosine catabolic process
GO:0006149
deoxyinosine catabolic process
GO:0006157
deoxyadenosine catabolic process
GO:0006166
purine ribonucleoside salvage
GO:0006204
IMP catabolic process
GO:0006738
nicotinamide riboside catabolic process
GO:0006955
immune response
GO:0009116
nucleoside metabolic process
GO:0009165
nucleotide biosynthetic process
GO:0009410
response to xenobiotic stimulus
GO:0032743
positive regulation of interleukin-2 production
GO:0034418
urate biosynthetic process
GO:0042102
positive regulation of T cell proliferation
GO:0043101
purine-containing compound salvage
GO:0046059
dAMP catabolic process
GO:0046638
positive regulation of alpha-beta T cell differentiation
Cellular Component
GO:0005576
extracellular region
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0034774
secretory granule lumen
GO:0070062
extracellular exosome
GO:1904813
ficolin-1-rich granule lumen
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1rt9
,
PDBe:1rt9
,
PDBj:1rt9
PDBsum
1rt9
PubMed
UniProt
P00491
|PNPH_HUMAN Purine nucleoside phosphorylase (Gene Name=PNP)
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