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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
ChainGOidnamespacecontents
A0006352biological_processDNA-templated transcription initiation
A0017025molecular_functionTBP-class protein binding
A0070897biological_processtranscription preinitiation complex assembly
B0003677molecular_functionDNA binding
B0006352biological_processDNA-templated transcription initiation
E0006352biological_processDNA-templated transcription initiation
E0017025molecular_functionTBP-class protein binding
E0070897biological_processtranscription preinitiation complex assembly
F0003677molecular_functionDNA binding
F0006352biological_processDNA-templated transcription initiation
I0006352biological_processDNA-templated transcription initiation
I0017025molecular_functionTBP-class protein binding
I0070897biological_processtranscription preinitiation complex assembly
J0003677molecular_functionDNA binding
J0006352biological_processDNA-templated transcription initiation
M0006352biological_processDNA-templated transcription initiation
M0017025molecular_functionTBP-class protein binding
M0070897biological_processtranscription preinitiation complex assembly
N0003677molecular_functionDNA binding
N0006352biological_processDNA-templated transcription initiation
Q0006352biological_processDNA-templated transcription initiation
Q0017025molecular_functionTBP-class protein binding
Q0070897biological_processtranscription preinitiation complex assembly
R0003677molecular_functionDNA binding
R0006352biological_processDNA-templated transcription initiation
Functional Information from PROSITE/UniProt
site_idPS00351
Number of Residues50
DetailsTFIID Transcription factor TFIID repeat signature. YnPkrFaaVImRirePRttaLIFsSGKMvctGAKseeqsrlAarkyarvV
ChainResidueDetails
BTYR192-VAL241
BTYR283-LEU332

site_idPS00782
Number of Residues16
DetailsTFIIB Transcription factor TFIIB repeat signature. GRandAIASACLYIAC
ChainResidueDetails
AGLY153-CYS168
AGLY247-SER262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsBINDING: BINDING => ECO:0000269|PubMed:27193682, ECO:0007744|PDB:5IYD
ChainResidueDetails
BASN167
FARG294
JASN167
JARG203
JLYS218
JASN257
JARG294
NASN167
NARG203
NLYS218
NASN257
BARG203
NARG294
RASN167
RARG203
RLYS218
RASN257
RARG294
ILYS272
IALA281
ITHR284
IARG286
BLYS218
IARG290
MLYS152
MARG154
MLYS189
MLYS196
MARG248
MLYS272
MALA281
MTHR284
MARG286
BASN257
MARG290
QLYS152
QARG154
QLYS189
QLYS196
QARG248
QLYS272
QALA281
QTHR284
QARG286
BARG294
QARG290
FASN167
FARG203
FLYS218
FASN257

site_idSWS_FT_FI2
Number of Residues5
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:12931194
ChainResidueDetails
ALYS238
ELYS238
ILYS238
MLYS238
QLYS238

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PDB entries from 2024-11-06

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