1C9B
CRYSTAL STRUCTURE OF A HUMAN TBP CORE DOMAIN-HUMAN TFIIB CORE DOMAIN COMPLEX BOUND TO AN EXTENDED, MODIFIED ADENOVIRAL MAJOR LATE PROMOTER (ADMLP)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006352 | biological_process | DNA-templated transcription initiation |
A | 0017025 | molecular_function | TBP-class protein binding |
A | 0070897 | biological_process | transcription preinitiation complex assembly |
B | 0003677 | molecular_function | DNA binding |
B | 0006352 | biological_process | DNA-templated transcription initiation |
E | 0006352 | biological_process | DNA-templated transcription initiation |
E | 0017025 | molecular_function | TBP-class protein binding |
E | 0070897 | biological_process | transcription preinitiation complex assembly |
F | 0003677 | molecular_function | DNA binding |
F | 0006352 | biological_process | DNA-templated transcription initiation |
I | 0006352 | biological_process | DNA-templated transcription initiation |
I | 0017025 | molecular_function | TBP-class protein binding |
I | 0070897 | biological_process | transcription preinitiation complex assembly |
J | 0003677 | molecular_function | DNA binding |
J | 0006352 | biological_process | DNA-templated transcription initiation |
M | 0006352 | biological_process | DNA-templated transcription initiation |
M | 0017025 | molecular_function | TBP-class protein binding |
M | 0070897 | biological_process | transcription preinitiation complex assembly |
N | 0003677 | molecular_function | DNA binding |
N | 0006352 | biological_process | DNA-templated transcription initiation |
Q | 0006352 | biological_process | DNA-templated transcription initiation |
Q | 0017025 | molecular_function | TBP-class protein binding |
Q | 0070897 | biological_process | transcription preinitiation complex assembly |
R | 0003677 | molecular_function | DNA binding |
R | 0006352 | biological_process | DNA-templated transcription initiation |
Functional Information from PROSITE/UniProt
site_id | PS00351 |
Number of Residues | 50 |
Details | TFIID Transcription factor TFIID repeat signature. YnPkrFaaVImRirePRttaLIFsSGKMvctGAKseeqsrlAarkyarvV |
Chain | Residue | Details |
B | TYR192-VAL241 | |
B | TYR283-LEU332 |
site_id | PS00782 |
Number of Residues | 16 |
Details | TFIIB Transcription factor TFIIB repeat signature. GRandAIASACLYIAC |
Chain | Residue | Details |
A | GLY153-CYS168 | |
A | GLY247-SER262 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 25 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27193682, ECO:0007744|PDB:5IYD |
Chain | Residue | Details |
B | ASN167 | |
F | ARG294 | |
J | ASN167 | |
J | ARG203 | |
J | LYS218 | |
J | ASN257 | |
J | ARG294 | |
N | ASN167 | |
N | ARG203 | |
N | LYS218 | |
N | ASN257 | |
B | ARG203 | |
N | ARG294 | |
R | ASN167 | |
R | ARG203 | |
R | LYS218 | |
R | ASN257 | |
R | ARG294 | |
I | LYS272 | |
I | ALA281 | |
I | THR284 | |
I | ARG286 | |
B | LYS218 | |
I | ARG290 | |
M | LYS152 | |
M | ARG154 | |
M | LYS189 | |
M | LYS196 | |
M | ARG248 | |
M | LYS272 | |
M | ALA281 | |
M | THR284 | |
M | ARG286 | |
B | ASN257 | |
M | ARG290 | |
Q | LYS152 | |
Q | ARG154 | |
Q | LYS189 | |
Q | LYS196 | |
Q | ARG248 | |
Q | LYS272 | |
Q | ALA281 | |
Q | THR284 | |
Q | ARG286 | |
B | ARG294 | |
Q | ARG290 | |
F | ASN167 | |
F | ARG203 | |
F | LYS218 | |
F | ASN257 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:12931194 |
Chain | Residue | Details |
A | LYS238 | |
E | LYS238 | |
I | LYS238 | |
M | LYS238 | |
Q | LYS238 |