Structure of PDB 1h52 Chain A Binding Site BS01

Receptor Information
>1h52 Chain A (length=122) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKR
SIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFR
NVVVACENGLPVHLDQSIFRRP
Ligand information
Ligand IDPOP
InChIInChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)/p-2
InChIKeyXPPKVPWEQAFLFU-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0O[P@@](=O)([O-])O[P@@](=O)(O)[O-]
CACTVS 3.341O[P]([O-])(=O)O[P](O)([O-])=O
ACDLabs 10.04[O-]P(=O)(O)OP([O-])(=O)O
OpenEye OEToolkits 1.5.0OP(=O)([O-])OP(=O)(O)[O-]
FormulaH2 O7 P2
NamePYROPHOSPHATE 2-
ChEMBL
DrugBank
ZINC
PDB chain1h52 Chain A Residue 1124 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1h52 Binding of Phosphate and Pyrophosphate Ions at the Active Site of Human Angiogenin as Revealed by X-Ray Crystallography
Resolution2.0 Å
Binding residue
(original residue number in PDB)		Q12 H13 K40 H114 L115 Q117
Binding residue
(residue number reindexed from 1)		Q11 H12 K39 H113 L114 Q116
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H13 K40 H114 L115 D116
Catalytic site (residue number reindexed from 1) H12 K39 H113 L114 D115
Enzyme Commision number 3.1.27.-
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0003779 actin binding
GO:0004519 endonuclease activity
GO:0004521 RNA endonuclease activity
GO:0004540 RNA nuclease activity
GO:0004549 tRNA-specific ribonuclease activity
GO:0005102 signaling receptor binding
GO:0005507 copper ion binding
GO:0005515 protein binding
GO:0008201 heparin binding
GO:0019843 rRNA binding
GO:0042277 peptide binding
GO:0042803 protein homodimerization activity
GO:0043022 ribosome binding
Biological Process
GO:0001525 angiogenesis
GO:0001541 ovarian follicle development
GO:0001556 oocyte maturation
GO:0001666 response to hypoxia
GO:0001890 placenta development
GO:0001938 positive regulation of endothelial cell proliferation
GO:0007154 cell communication
GO:0009303 rRNA transcription
GO:0009725 response to hormone
GO:0016078 tRNA decay
GO:0016477 cell migration
GO:0017148 negative regulation of translation
GO:0019731 antibacterial humoral response
GO:0023052 signaling
GO:0030041 actin filament polymerization
GO:0030154 cell differentiation
GO:0032055 negative regulation of translation in response to stress
GO:0034063 stress granule assembly
GO:0042327 positive regulation of phosphorylation
GO:0042592 homeostatic process
GO:0043066 negative regulation of apoptotic process
GO:0045087 innate immune response
GO:0048662 negative regulation of smooth muscle cell proliferation
GO:0050714 positive regulation of protein secretion
GO:0050830 defense response to Gram-positive bacterium
GO:0061844 antimicrobial humoral immune response mediated by antimicrobial peptide
GO:0071425 hematopoietic stem cell proliferation
Cellular Component
GO:0005576 extracellular region
GO:0005604 basement membrane
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005694 chromosome
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0010494 cytoplasmic stress granule
GO:0015629 actin cytoskeleton
GO:0030139 endocytic vesicle
GO:0030426 growth cone
GO:0031410 cytoplasmic vesicle
GO:0032311 angiogenin-PRI complex
GO:0043025 neuronal cell body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h52, PDBe:1h52, PDBj:1h52
PDBsum1h52
PubMed11468363
UniProtP03950|ANGI_HUMAN Angiogenin (Gene Name=ANG)

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