3V61
Structure of S. cerevisiae PCNA conjugated to SUMO on lysine 164
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000278 | biological_process | mitotic cell cycle |
| B | 0000710 | biological_process | meiotic mismatch repair |
| B | 0000781 | cellular_component | chromosome, telomeric region |
| B | 0003677 | molecular_function | DNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005657 | cellular_component | replication fork |
| B | 0006260 | biological_process | DNA replication |
| B | 0006272 | biological_process | leading strand elongation |
| B | 0006273 | biological_process | lagging strand elongation |
| B | 0006275 | biological_process | regulation of DNA replication |
| B | 0006281 | biological_process | DNA repair |
| B | 0006289 | biological_process | nucleotide-excision repair |
| B | 0006298 | biological_process | mismatch repair |
| B | 0006301 | biological_process | postreplication repair |
| B | 0007064 | biological_process | mitotic sister chromatid cohesion |
| B | 0019985 | biological_process | translesion synthesis |
| B | 0030337 | molecular_function | DNA polymerase processivity factor activity |
| B | 0030466 | biological_process | silent mating-type cassette heterochromatin formation |
| B | 0031509 | biological_process | subtelomeric heterochromatin formation |
| B | 0034087 | biological_process | establishment of mitotic sister chromatid cohesion |
| B | 0035753 | biological_process | maintenance of DNA trinucleotide repeats |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043626 | cellular_component | PCNA complex |
| B | 0045739 | biological_process | positive regulation of DNA repair |
| B | 0045740 | biological_process | positive regulation of DNA replication |
| B | 0051054 | biological_process | positive regulation of DNA metabolic process |
| B | 0070987 | biological_process | error-free translesion synthesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BA A 2 |
| Chain | Residue |
| A | HOH6 |
| A | ASP82 |
| A | ASP85 |
| A | HOH100 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BA A 3 |
| Chain | Residue |
| A | ASP87 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BA A 4 |
| Chain | Residue |
| A | HIS23 |
| A | ASP82 |
| A | ASP85 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BA A 11 |
| Chain | Residue |
| B | ASP33 |
| A | HOH113 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BA B 259 |
| Chain | Residue |
| B | ASP21 |
| B | ASP214 |
| B | HOH275 |
| B | HOH280 |
| B | HOH323 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BA B 260 |
| Chain | Residue |
| B | ASP240 |
| B | LEU241 |
| B | HOH270 |
| B | HOH273 |
| B | HOH322 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BA B 261 |
| Chain | Residue |
| B | PHE57 |
| B | BA262 |
| B | HOH299 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BA B 262 |
| Chain | Residue |
| B | GLU55 |
| B | BA261 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BA B 263 |
| Chain | Residue |
| B | GLU7 |
| B | THR85 |
| B | THR87 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BA B 264 |
| Chain | Residue |
| B | ASP93 |
| B | ASN94 |
| B | THR95 |
| B | HOH340 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BA B 265 |
| Chain | Residue |
| A | HOH108 |
| B | HOH293 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BA B 266 |
| Chain | Residue |
| B | ASP172 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BA B 267 |
| Chain | Residue |
| B | ARG80 |
| B | GLY82 |
| B | HOH274 |
| B | HOH276 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NEQ B 268 |
| Chain | Residue |
| B | GLY18 |
| B | PHE19 |
| B | CYS22 |
| B | VAL48 |
| B | ASP214 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NEQ B 269 |
| Chain | Residue |
| B | ILE78 |
| B | CYS81 |
| B | ASP150 |
| B | GLN153 |
| B | LEU154 |
| B | HOH324 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 19 |
| Details | DNA_BIND: DNA_BIND => ECO:0000255 |
| Chain | Residue | Details |
| B | ARG61-ARG80 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15166219 |
| Chain | Residue | Details |
| B | GLY127 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:12226657 |
| Chain | Residue | Details |
| B | LYS164 |
