Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9EI2

Cryo-EM structure of Human RNA polymerase II Elongation Complex bound to an apo RECQL5 helicase (RECQL5 IRI Module focused-classified)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000428cellular_componentDNA-directed RNA polymerase complex
A0000974cellular_componentPrp19 complex
A0001172biological_processRNA-templated transcription
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0003899molecular_functionDNA-directed RNA polymerase activity
A0003968molecular_functionRNA-directed RNA polymerase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005665cellular_componentRNA polymerase II, core complex
A0005694cellular_componentchromosome
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0006353biological_processDNA-templated transcription termination
A0006355biological_processregulation of DNA-templated transcription
A0006366biological_processtranscription by RNA polymerase II
A0006368biological_processtranscription elongation by RNA polymerase II
A0008270molecular_functionzinc ion binding
A0010628biological_processpositive regulation of gene expression
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0016787molecular_functionhydrolase activity
A0019900molecular_functionkinase binding
A0031625molecular_functionubiquitin protein ligase binding
A0033120biological_processpositive regulation of RNA splicing
A0034062molecular_function5'-3' RNA polymerase activity
A0042789biological_processmRNA transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0050436molecular_functionmicrofibril binding
A1990841molecular_functionpromoter-specific chromatin binding
U0000166molecular_functionnucleotide binding
U0000278biological_processmitotic cell cycle
U0000724biological_processdouble-strand break repair via homologous recombination
U0000993molecular_functionRNA polymerase II complex binding
U0003677molecular_functionDNA binding
U0003678molecular_functionDNA helicase activity
U0004386molecular_functionhelicase activity
U0005524molecular_functionATP binding
U0005634cellular_componentnucleus
U0005654cellular_componentnucleoplasm
U0005657cellular_componentreplication fork
U0005694cellular_componentchromosome
U0005737cellular_componentcytoplasm
U0005829cellular_componentcytosol
U0006259biological_processDNA metabolic process
U0006260biological_processDNA replication
U0006281biological_processDNA repair
U0006974biological_processDNA damage response
U0009378molecular_functionfour-way junction helicase activity
U0010605biological_processnegative regulation of macromolecule metabolic process
U0016787molecular_functionhydrolase activity
U0016853molecular_functionisomerase activity
U0016887molecular_functionATP hydrolysis activity
U0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
U0043138molecular_function3'-5' DNA helicase activity
U0045934biological_processnegative regulation of nucleobase-containing compound metabolic process
U0046872molecular_functionmetal ion binding
U0051301biological_processcell division
U0051304biological_processchromosome separation
U0071466biological_processcellular response to xenobiotic stimulus
U0072757biological_processcellular response to camptothecin
U0097550cellular_componenttranscription preinitiation complex
U0140097molecular_functioncatalytic activity, acting on DNA
U1990414biological_processreplication-born double-strand break repair via sister chromatid exchange
U1990506biological_processmitotic DNA-templated DNA replication
U2000042biological_processnegative regulation of double-strand break repair via homologous recombination
Functional Information from PROSITE/UniProt
site_idPS00115
Number of Residues7
DetailsRNA_POL_II_REPEAT Eukaryotic RNA polymerase II heptapeptide repeat. YSPTSPA
ChainResidueDetails
ATYR1593-ALA1599
ATYR1671-SER1677
ATYR1678-SER1684
ATYR1685-SER1691
ATYR1692-SER1698
ATYR1699-SER1705
ATYR1706-SER1712
ATYR1713-SER1719
ATYR1720-SER1726
ATYR1727-SER1733
ATYR1734-SER1740
ATYR1615-SER1621
ATYR1741-ASN1747
ATYR1748-ASN1754
ATYR1755-SER1761
ATYR1762-SER1768
ATYR1769-ASN1775
ATYR1776-ASN1782
ATYR1783-SER1789
ATYR1790-SER1796
ATYR1797-SER1803
ATYR1818-SER1824
ATYR1622-SER1628
ATYR1825-SER1831
ATYR1839-SER1845
ATYR1853-LYS1859
ATYR1860-LYS1866
ATYR1867-LYS1873
ATYR1874-THR1880
ATYR1888-THR1894
ATYR1902-LYS1908
ATYR1909-THR1915
ATYR1916-LYS1922
ATYR1629-ASN1635
ATYR1923-THR1929
ATYR1930-LYS1936
ATYR1947-THR1953
ATYR1636-SER1642
ATYR1643-SER1649
ATYR1650-SER1656
ATYR1657-SER1663
ATYR1664-SER1670

site_idPS00690
Number of Residues10
DetailsDEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. SyLVVDEAHC
ChainResidueDetails
USER152-CYS161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000305|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA
ChainResidueDetails
UPHE26
USER28
ULYS30
UGLN34
UGLY55
UALA56
UGLY57
ULYS58
USER59

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:5LB5
ChainResidueDetails
UPRO53
AASP495
ACYS74
ACYS81
AHIS84
ACYS111
ACYS114
ACYS154
ACYS184
AASN493

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LB8, ECO:0007744|PDB:5LBA
ChainResidueDetails
UCYS411
UCYS431
UCYS434

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA
ChainResidueDetails
UCYS427

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:D4ACP5
ChainResidueDetails
USER488
ASER217
ASER1868

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
USER491

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:28575661, ECO:0007744|PubMed:23186163
ChainResidueDetails
USER727

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
USER815

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
UTHR839
ATHR1933
ATHR1863
ATHR1870
ATHR1877
ATHR1912
ATHR1915
ATHR1919
ATHR1926
ATHR1929

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26566685, ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER1843

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26566685
ChainResidueDetails
ASER1845
ASER1857
ASER1861
ASER1875

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P08775
ChainResidueDetails
ASER1847

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26566685, ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER1849

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26566685, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1850
ASER1864

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR1854

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:26566685
ChainResidueDetails
ALYS1859
ALYS1866
ALYS1873
ALYS1887

site_idSWS_FT_FI17
Number of Residues5
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:26566685
ChainResidueDetails
ATYR1860
ATYR1867
ATYR1881
ATYR1916
ATYR1930

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:26566685, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATYR1874

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26566685, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1878
ASER1882

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR1885

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P08775
ChainResidueDetails
ATHR1894

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER1896

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1899

site_idSWS_FT_FI24
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1906

site_idSWS_FT_FI25
Number of Residues1
DetailsMOD_RES: N6,N6-dimethyllysine => ECO:0000250|UniProtKB:P08775
ChainResidueDetails
ALYS1908

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:26566685, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATYR1909
ATYR1923

site_idSWS_FT_FI27
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26566685, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1913
ASER1920
ASER1927

site_idSWS_FT_FI28
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26566685, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER1917
ASER1931

site_idSWS_FT_FI29
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:26566685
ChainResidueDetails
ALYS1922
ALYS1936

site_idSWS_FT_FI30
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1934

site_idSWS_FT_FI31
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); by NEDD4 => ECO:0000269|PubMed:32142649, ECO:0000305|PubMed:32142654
ChainResidueDetails
ALYS1268

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon