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4W5N

The Crystal Structure of Human Argonaute2 Bound to a Defined Guide RNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000340molecular_functionRNA 7-methylguanosine cap binding
A0000932cellular_componentP-body
A0000993molecular_functionRNA polymerase II complex binding
A0001046molecular_functioncore promoter sequence-specific DNA binding
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0003725molecular_functiondouble-stranded RNA binding
A0003727molecular_functionsingle-stranded RNA binding
A0003729molecular_functionmRNA binding
A0003743molecular_functiontranslation initiation factor activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006355biological_processregulation of DNA-templated transcription
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0006417biological_processregulation of translation
A0009791biological_processpost-embryonic development
A0010501biological_processRNA secondary structure unwinding
A0010586biological_processmiRNA metabolic process
A0010628biological_processpositive regulation of gene expression
A0016020cellular_componentmembrane
A0016442cellular_componentRISC complex
A0016787molecular_functionhydrolase activity
A0016891molecular_functionRNA endonuclease activity, producing 5'-phosphomonoesters
A0030422biological_processsiRNA processing
A0030425cellular_componentdendrite
A0031047biological_processregulatory ncRNA-mediated gene silencing
A0031054biological_processpre-miRNA processing
A0035194biological_processregulatory ncRNA-mediated post-transcriptional gene silencing
A0035196biological_processmiRNA processing
A0035197molecular_functionsiRNA binding
A0035198molecular_functionmiRNA binding
A0035278biological_processmiRNA-mediated gene silencing by inhibition of translation
A0035279biological_processmiRNA-mediated gene silencing by mRNA destabilization
A0035925molecular_functionmRNA 3'-UTR AU-rich region binding
A0036464cellular_componentcytoplasmic ribonucleoprotein granule
A0042985biological_processnegative regulation of amyloid precursor protein biosynthetic process
A0045727biological_processpositive regulation of translation
A0045766biological_processpositive regulation of angiogenesis
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0045947biological_processnegative regulation of translational initiation
A0046872molecular_functionmetal ion binding
A0060213biological_processpositive regulation of nuclear-transcribed mRNA poly(A) tail shortening
A0061980molecular_functionregulatory RNA binding
A0070062cellular_componentextracellular exosome
A0070551molecular_functionendoribonuclease activity, cleaving siRNA-paired mRNA
A0070578cellular_componentRISC-loading complex
A0070922biological_processRISC complex assembly
A0090624molecular_functionendoribonuclease activity, cleaving miRNA-paired mRNA
A0090625biological_processsiRNA-mediated gene silencing by mRNA destabilization
A0098808molecular_functionmRNA cap binding
A1900153biological_processpositive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
A1901165biological_processpositive regulation of trophoblast cell migration
A1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue IPH A 901
ChainResidue
APHE587
AGLN589
AVAL591
AALA620
APHE653

site_idAC2
Number of Residues4
Detailsbinding site for residue IPH A 902
ChainResidue
ALEU650
ALYS660
ALEU694
ATYR698

site_idAC3
Number of Residues4
Detailsbinding site for residue IPH A 903
ChainResidue
ATYR174
APHE200
AGLY201
ALEU382

site_idAC4
Number of Residues2
Detailsbinding site for residue MG A 904
ChainResidue
AASP597
AVAL598

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP597
AASP669
AHIS807

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q8CJG0, ECO:0000255|HAMAP-Rule:MF_03031
ChainResidueDetails
ATYR2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:23603119, ECO:0007744|PubMed:23186163
ChainResidueDetails
AASP387

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 4-hydroxyproline => ECO:0000255|HAMAP-Rule:MF_03031, ECO:0000269|PubMed:18690212
ChainResidueDetails
APRO700

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:28114302
ChainResidueDetails
ASER824
ASER831
ASER834

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:28114302, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER828

218853

PDB entries from 2024-04-24

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