6DCF
Crystal structure of a Mycobacterium smegmatis transcription initiation complex with Rifampicin-resistant RNA polymerase and bound to kanglemycin A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
A | 0003677 | molecular_function | DNA binding |
A | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006351 | biological_process | DNA-templated transcription |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
A | 0046983 | molecular_function | protein dimerization activity |
B | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
B | 0003677 | molecular_function | DNA binding |
B | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006351 | biological_process | DNA-templated transcription |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
B | 0046983 | molecular_function | protein dimerization activity |
C | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
C | 0003677 | molecular_function | DNA binding |
C | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
C | 0005515 | molecular_function | protein binding |
C | 0006351 | biological_process | DNA-templated transcription |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0032549 | molecular_function | ribonucleoside binding |
C | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
C | 0046677 | biological_process | response to antibiotic |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
D | 0003677 | molecular_function | DNA binding |
D | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
D | 0006351 | biological_process | DNA-templated transcription |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016779 | molecular_function | nucleotidyltransferase activity |
D | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
E | 0003677 | molecular_function | DNA binding |
E | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
E | 0006351 | biological_process | DNA-templated transcription |
E | 0016779 | molecular_function | nucleotidyltransferase activity |
E | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
F | 0003677 | molecular_function | DNA binding |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006352 | biological_process | DNA-templated transcription initiation |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0010468 | biological_process | regulation of gene expression |
F | 0016987 | molecular_function | sigma factor activity |
F | 2000142 | biological_process | regulation of DNA-templated transcription initiation |
J | 0001000 | molecular_function | bacterial-type RNA polymerase core enzyme binding |
J | 0045893 | biological_process | positive regulation of DNA-templated transcription |
J | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue KNG C 1201 |
Chain | Residue |
C | GLY423 |
C | ILE488 |
C | ARG604 |
C | SER425 |
C | GLN426 |
C | SER428 |
C | GLN429 |
C | PHE430 |
C | ASP432 |
C | HIS442 |
C | ARG445 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 1202 |
Chain | Residue |
C | HIS720 |
C | ARG1005 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 1203 |
Chain | Residue |
C | ARG595 |
C | ARG916 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 1204 |
Chain | Residue |
C | HIS832 |
C | ILE1032 |
C | HIS1033 |
C | ALA1034 |
C | GLN1053 |
C | PHE1054 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN D 2001 |
Chain | Residue |
D | CYS890 |
D | CYS967 |
D | CYS974 |
D | CYS977 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN D 2002 |
Chain | Residue |
D | CYS60 |
D | CYS62 |
D | CYS75 |
D | CYS78 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue MG D 2003 |
Chain | Residue |
D | ASP535 |
D | ASP537 |
D | ASP539 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue SO4 D 2004 |
Chain | Residue |
D | HIS888 |
D | ARG1267 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue SO4 D 2005 |
Chain | Residue |
D | ARG421 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 2006 |
Chain | Residue |
D | ASP882 |
D | THR971 |
D | GLY972 |
D | ARG1160 |
D | ARG1164 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue SO4 D 2007 |
Chain | Residue |
D | ARG894 |
D | GLY895 |
D | LYS960 |
D | ARG1129 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue GLU D 2008 |
Chain | Residue |
D | ARG886 |
D | PRO1260 |
D | ILE1265 |
D | SER1266 |
D | ARG1267 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue SO4 F 501 |
Chain | Residue |
F | ALA254 |
F | PHE255 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue SO4 F 502 |
Chain | Residue |
D | VAL592 |
D | SER628 |
D | ARG630 |
F | LYS210 |
F | LEU211 |
F | VAL213 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue EDO F 503 |
Chain | Residue |
F | GLN291 |
F | ALA292 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue EDO F 504 |
Chain | Residue |
F | ARG224 |
F | ASP225 |
F | ARG228 |
Functional Information from PROSITE/UniProt
site_id | PS00715 |
Number of Residues | 14 |
Details | SIGMA70_1 Sigma-70 factors family signature 1. DLIQeGnLGLIrAV |
Chain | Residue | Details |
F | ASP257-VAL270 |
site_id | PS00716 |
Number of Residues | 27 |
Details | SIGMA70_2 Sigma-70 factors family signature 2. TldEIGqvygVTrerIrQIEsktMskL |
Chain | Residue | Details |
F | THR426-LEU452 |
site_id | PS00867 |
Number of Residues | 8 |
Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLEANLRL |
Chain | Residue | Details |
F | LEU233-LEU240 |
site_id | PS01166 |
Number of Residues | 13 |
Details | RNA_POL_BETA RNA polymerases beta chain signature. GdKLAGrHGNKGV |
Chain | Residue | Details |
C | GLY873-VAL885 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 11 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01322 |
Chain | Residue | Details |
D | CYS60 | |
D | CYS974 | |
D | CYS977 | |
D | CYS62 | |
D | CYS75 | |
D | CYS78 | |
D | ASP535 | |
D | ASP537 | |
D | ASP539 | |
D | CYS890 | |
D | CYS967 |