8S54
RNA polymerase II early elongation complex bound to TFIIE and TFIIF - state b (composite structure)
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_id | PS01154 |
Number of Residues | 32 |
Details | RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. InkEdHTLgNiIksqLlkdpqVlfagYkvpHP |
Chain | Residue | Details |
K | ILE35-PRO66 |
site_id | PS01110 |
Number of Residues | 14 |
Details | RNA_POL_H_23KD RNA polymerases H / 23 Kd subunits signature. HELVPEHvvMtkEE |
Chain | Residue | Details |
E | HIS142-GLU155 |
site_id | PS00115 |
Number of Residues | 7 |
Details | RNA_POL_II_REPEAT Eukaryotic RNA polymerase II heptapeptide repeat. YSPTSPA |
Chain | Residue | Details |
A | TYR1593-ALA1599 | |
A | TYR1615-SER1621 | |
A | TYR1622-SER1628 | |
A | TYR1629-ASN1635 | |
A | TYR1636-SER1642 | |
A | TYR1643-SER1649 | |
A | TYR1650-SER1656 | |
A | TYR1657-SER1663 | |
A | TYR1664-SER1670 | |
A | TYR1671-SER1677 | |
A | TYR1678-SER1684 | |
A | TYR1685-SER1691 | |
A | TYR1692-SER1698 | |
A | TYR1699-SER1705 | |
A | TYR1706-SER1712 | |
A | TYR1713-SER1719 | |
A | TYR1720-SER1726 | |
A | TYR1727-SER1733 | |
A | TYR1734-SER1740 | |
A | TYR1741-SER1747 | |
A | TYR1748-SER1754 | |
A | TYR1755-ASN1761 | |
A | TYR1762-ASN1768 | |
A | TYR1769-SER1775 | |
A | TYR1776-SER1782 | |
A | TYR1783-ASN1789 | |
A | TYR1790-ASN1796 | |
A | TYR1797-SER1803 | |
A | TYR1804-SER1810 | |
A | TYR1811-SER1817 | |
A | TYR1832-SER1838 | |
A | TYR1839-SER1845 | |
A | TYR1846-LYS1852 | |
A | TYR1853-SER1859 | |
A | TYR1867-LYS1873 | |
A | TYR1874-LYS1880 | |
A | TYR1881-LYS1887 | |
A | TYR1888-THR1894 | |
A | TYR1902-THR1908 | |
A | TYR1916-LYS1922 | |
A | TYR1923-THR1929 | |
A | TYR1930-LYS1936 | |
A | TYR1937-THR1943 | |
A | TYR1944-LYS1950 | |
A | TYR1961-THR1967 |
site_id | PS01111 |
Number of Residues | 15 |
Details | RNA_POL_K_14KD RNA polymerases K / 14 to 18 Kd subunits signature. TkYErARvLGtRAlQ |
Chain | Residue | Details |
F | THR58-GLN72 |
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YVCTAPH |
Chain | Residue | Details |
I | TYR112-HIS118 |
site_id | PS00466 |
Number of Residues | 38 |
Details | ZF_TFIIS_1 Zinc finger TFIIS-type signature. CqkCghkeavffqSHSARaEDAmrlyyvCtaph.CghrW |
Chain | Residue | Details |
I | CYS86-TRP123 |
site_id | PS01030 |
Number of Residues | 27 |
Details | RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCqECNNMLypkedkenrillyaCrnC |
Chain | Residue | Details |
I | PHE16-CYS42 |
site_id | PS01112 |
Number of Residues | 10 |
Details | RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IIPVrCFTCG |
Chain | Residue | Details |
J | ILE2-GLY11 |
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DNDPSDYVEqdDI |
Chain | Residue | Details |
C | ASP136-ILE148 |
site_id | PS00446 |
Number of Residues | 41 |
Details | RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NSIRRvfiaevpiiAidwVqidaNsSvlhDEfIAhRLGLIP |
Chain | Residue | Details |
C | ASN32-PRO72 |
site_id | PS01166 |
Number of Residues | 13 |
Details | RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT |
Chain | Residue | Details |
B | GLY932-THR944 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | ZN_FING: C4-type => ECO:0000255 |
Chain | Residue | Details |
R | HIS229 | |
Q | GLU517 | |
W | CYS129-CYS157 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27193682, ECO:0007744|PDB:5IY6 |
Chain | Residue | Details |
W | CYS132 | |
W | CYS154 | |
W | CYS157 | |
W | CYS129 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
I | CYS42 | |
W | ALA2 | |
R | LYS33 | |
R | LYS137 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
I | CYS89 | |
I | CYS114 | |
I | CYS119 | |
W | LYS67 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
Q | SER224 | |
W | SER268 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
Q | SER221 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
Q | THR331 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
Q | SER377 | |
Q | SER431 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
Q | SER380 | |
Q | SER381 | |
Q | SER436 | |
Q | SER449 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:10428810, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
Q | SER385 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:10428810, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
Q | THR389 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
Q | SER391 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
Q | LYS407 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
Q | SER433 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
Q | THR446 |