2ZVV
Crystal structure of Proliferating cellular nuclear antigen 1 and Short peptide from human P21
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005730 | cellular_component | nucleolus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006260 | biological_process | DNA replication |
A | 0006272 | biological_process | leading strand elongation |
A | 0006275 | biological_process | regulation of DNA replication |
A | 0006298 | biological_process | mismatch repair |
A | 0019985 | biological_process | translesion synthesis |
A | 0030337 | molecular_function | DNA polymerase processivity factor activity |
A | 0043626 | cellular_component | PCNA complex |
A | 0051726 | biological_process | regulation of cell cycle |
B | 0003677 | molecular_function | DNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005730 | cellular_component | nucleolus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006260 | biological_process | DNA replication |
B | 0006272 | biological_process | leading strand elongation |
B | 0006275 | biological_process | regulation of DNA replication |
B | 0006298 | biological_process | mismatch repair |
B | 0019985 | biological_process | translesion synthesis |
B | 0030337 | molecular_function | DNA polymerase processivity factor activity |
B | 0043626 | cellular_component | PCNA complex |
B | 0051726 | biological_process | regulation of cell cycle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 901 |
Chain | Residue |
A | ASP156 |
A | ALA208 |
A | ARG210 |
A | LYS254 |
A | HOH1013 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 911 |
Chain | Residue |
B | HOH1029 |
B | HOH1207 |
B | ASP156 |
B | ALA208 |
B | ARG210 |
B | LYS254 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 38 |
Details | DNA binding: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2","evidences":[{"source":"PubMed","id":"10753973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11463845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12431783","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16982699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20307683","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine; by PKC and NUAK1","evidences":[{"source":"PubMed","id":"10753973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25329316","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |