Structure of PDB 2bwk Chain A Binding Site BS01
Receptor Information
>2bwk Chain A (length=117) Species:
10090
(Mus musculus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
DSRYTKFLTQHHDAKPKGRDDRYCERMMKRRSLTSPCKDVNTFIHGNKSN
IKAICGANGSPYRENLRMSKSPFQVTTCKHTGGSPRPPCQYRASAGFRHV
VIACENGLPVHFDESFF
Ligand information
Ligand ID
SO4
InChI
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKey
QAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
[O-]S(=O)(=O)[O-]
CACTVS 3.341
[O-][S]([O-])(=O)=O
ACDLabs 10.04
[O-]S([O-])(=O)=O
Formula
O4 S
Name
SULFATE ION
ChEMBL
DrugBank
DB14546
ZINC
PDB chain
2bwk Chain A Residue 1121 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
2bwk
Structure of Murine Angiogenin: Features of the Substrate- and Cell-Binding Regions and Prospects for Inhibitor-Binding Studies.
Resolution
1.5 Å
Binding residue
(original residue number in PDB)
H13 H113 S117 F119
Binding residue
(residue number reindexed from 1)
H11 H111 S115 F117
Annotation score
3
Enzymatic activity
Catalytic site (original residue number in PDB)
H13 K40 H113 F114 D115
Catalytic site (residue number reindexed from 1)
H11 K38 H111 F112 D113
Enzyme Commision number
3.1.27.-
Gene Ontology
Molecular Function
GO:0003676
nucleic acid binding
GO:0003677
DNA binding
GO:0003723
RNA binding
GO:0003779
actin binding
GO:0004519
endonuclease activity
GO:0004540
RNA nuclease activity
GO:0004549
tRNA-specific ribonuclease activity
GO:0005102
signaling receptor binding
GO:0005507
copper ion binding
GO:0008201
heparin binding
GO:0042803
protein homodimerization activity
Biological Process
GO:0001525
angiogenesis
GO:0001666
response to hypoxia
GO:0001938
positive regulation of endothelial cell proliferation
GO:0007417
central nervous system development
GO:0009303
rRNA transcription
GO:0017148
negative regulation of translation
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:0036417
tRNA destabilization
GO:0043066
negative regulation of apoptotic process
GO:0048662
negative regulation of smooth muscle cell proliferation
GO:0050714
positive regulation of protein secretion
GO:0071425
hematopoietic stem cell proliferation
GO:0071470
cellular response to osmotic stress
GO:2000773
negative regulation of cellular senescence
Cellular Component
GO:0005576
extracellular region
GO:0005604
basement membrane
GO:0005615
extracellular space
GO:0005634
nucleus
GO:0005730
nucleolus
GO:0005737
cytoplasm
GO:0030139
endocytic vesicle
GO:0030426
growth cone
GO:0031410
cytoplasmic vesicle
GO:0032311
angiogenin-PRI complex
GO:0043025
neuronal cell body
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:2bwk
,
PDBe:2bwk
,
PDBj:2bwk
PDBsum
2bwk
PubMed
16301790
UniProt
P21570
|ANGI_MOUSE Angiogenin (Gene Name=Ang)
[
Back to BioLiP
]