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4OAU

Complete human RNase L in complex with biological activators.

Functional Information from GO Data
ChainGOidnamespacecontents
C0003723molecular_functionRNA binding
C0004519molecular_functionendonuclease activity
C0004521molecular_functionRNA endonuclease activity
C0004540molecular_functionRNA nuclease activity
C0004672molecular_functionprotein kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005829cellular_componentcytosol
C0006364biological_processrRNA processing
C0006396biological_processRNA processing
C0006397biological_processmRNA processing
C0006468biological_processprotein phosphorylation
C0016363cellular_componentnuclear matrix
C0019843molecular_functionrRNA binding
C0043021molecular_functionribonucleoprotein complex binding
C0043488biological_processregulation of mRNA stability
C0045071biological_processnegative regulation of viral genome replication
C0045444biological_processfat cell differentiation
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0046326biological_processpositive regulation of D-glucose import
C0046872molecular_functionmetal ion binding
C0051607biological_processdefense response to virus
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ADP C 801
ChainResidue
CILE371
CTHR440
CGLN489
CASN490
CLEU492
CASP503
CASP505
CMG802
CMG803
CHOH923
CHOH925
CALA372
CHOH993
CTHR374
CILE379
CALA390
CLYS392
CVAL434
CTHR435
CCYS437

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 802
ChainResidue
CGLN487
CASN490
CASP503
CADP801
CMG803
CHOH923

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 803
ChainResidue
CASP503
CASP505
CADP801
CMG802

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues49
DetailsZN_FING: C6-type; atypical
ChainResidueDetails
CCYS395-CYS444

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS684

227111

PDB entries from 2024-11-06

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