1MK2
SMAD3 SBD complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY A 1 |
Chain | Residue |
A | PRO317 |
A | ASN320 |
A | PRO327 |
A | ALA328 |
A | ARG367 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACY A 2 |
Chain | Residue |
A | TRP379 |
A | GLN386 |
A | THR387 |
A | VAL388 |
A | GLN315 |
A | HIS326 |
A | PRO327 |
A | ARG372 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY A 3 |
Chain | Residue |
A | GLU382 |
A | ARG384 |
B | ASN673 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 4 |
Chain | Residue |
A | ASN264 |
A | SER265 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:16862174 |
Chain | Residue | Details |
A | LYS377 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER415 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CK1 => ECO:0000255|PROSITE-ProRule:PRU00439, ECO:0000269|PubMed:18794808 |
Chain | Residue | Details |
A | SER417 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine; by TGFBR1 => ECO:0000250|UniProtKB:Q8BUN5, ECO:0000255|PROSITE-ProRule:PRU00439 |
Chain | Residue | Details |
A | SER421 | |
A | SER422 | |
A | SER424 |