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4RWQ

Crystal structure of the apo-state of porcine OAS1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001730molecular_function2'-5'-oligoadenylate synthetase activity
A0003723molecular_functionRNA binding
A0003725molecular_functiondouble-stranded RNA binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0016020cellular_componentmembrane
A0016779molecular_functionnucleotidyltransferase activity
A0045071biological_processnegative regulation of viral genome replication
A0045087biological_processinnate immune response
A0046872molecular_functionmetal ion binding
A0051607biological_processdefense response to virus
A0060700biological_processregulation of ribonuclease activity
A1904188biological_processnegative regulation of transformation of host cell by virus
B0001730molecular_function2'-5'-oligoadenylate synthetase activity
B0003723molecular_functionRNA binding
B0003725molecular_functiondouble-stranded RNA binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0016020cellular_componentmembrane
B0016779molecular_functionnucleotidyltransferase activity
B0045071biological_processnegative regulation of viral genome replication
B0045087biological_processinnate immune response
B0046872molecular_functionmetal ion binding
B0051607biological_processdefense response to virus
B0060700biological_processregulation of ribonuclease activity
B1904188biological_processnegative regulation of transformation of host cell by virus
Functional Information from PROSITE/UniProt
site_idPS00832
Number of Residues20
Details25A_SYNTH_1 2'-5'-oligoadenylate synthases signature 1. GSsGKgTtLRgrsDaDLVvF
ChainResidueDetails
AGLY61-PHE80

site_idPS00833
Number of Residues11
Details25A_SYNTH_2 2'-5'-oligoadenylate synthases signature 2. RPVILDPaDPT
ChainResidueDetails
AARG295-THR305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00973
ChainResidueDetails
ASER62
BGLN229
AASP74
AASP76
AASP147
AGLN229
BSER62
BASP74
BASP76
BASP147

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:18604630
ChainResidueDetails
AARG209
BARG209

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:14636576
ChainResidueDetails
ALYS212
BLYS212

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Interaction with dsRNA => ECO:0000250|UniProtKB:P00973
ChainResidueDetails
AGLN157
BGLN157

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PDB entries from 2024-07-24

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