2C62
Crystal Structure of the Human Transcription Cofactor PC4 in Complex with Single-Stranded DNA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003713 | molecular_function | transcription coactivator activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0060261 | biological_process | positive regulation of transcription initiation by RNA polymerase II |
B | 0003677 | molecular_function | DNA binding |
B | 0003713 | molecular_function | transcription coactivator activity |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0060261 | biological_process | positive regulation of transcription initiation by RNA polymerase II |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A1128 |
Chain | Residue |
A | ALA62 |
A | HOH2054 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C1021 |
Chain | Residue |
C | DG20 |
C | HOH2049 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | MET69 | |
B | MET69 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | ASP119 | |
B | ASP119 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | MET69 | |
B | MET69 |