Structure of PDB 1hi2 Chain A

Receptor sequence
>1hi2A (length=135) Species: 9606 (Homo sapiens) [Search protein sequence]
MKPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTFLLTTFA
NVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYA
QTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII
3D structure
PDB1hi2 Mapping the Ribonucleolytic Active Site of Eosinophil-Derived Neurotoxin (Edn): High Resolution Crystal Structures of Edn Complexes with Adenylic Nucleotide Inhibitors
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) H15 K38 H129
Catalytic site (residue number reindexed from 1) H16 K39 H130
Enzyme Commision number 4.6.1.18: pancreatic ribonuclease.
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 SO4 A H15 H129 H16 H130
BS02 SO4 A R36 K38 N39 Q40 R37 K39 N40 Q41
Gene Ontology
Molecular Function
GO:0001530 lipopolysaccharide binding
GO:0003676 nucleic acid binding
GO:0004519 endonuclease activity
GO:0004522 ribonuclease A activity
GO:0004540 RNA nuclease activity
GO:0005515 protein binding
GO:0016829 lyase activity
Biological Process
GO:0002227 innate immune response in mucosa
GO:0006401 RNA catabolic process
GO:0006935 chemotaxis
GO:0043152 induction of bacterial agglutination
GO:0050829 defense response to Gram-negative bacterium
GO:0050830 defense response to Gram-positive bacterium
GO:0051607 defense response to virus
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005764 lysosome
GO:0035578 azurophil granule lumen
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1hi2, PDBe:1hi2, PDBj:1hi2
PDBsum1hi2
PubMed11154698
UniProtP10153|RNAS2_HUMAN Non-secretory ribonuclease (Gene Name=RNASE2)

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