2IJX
Crystal structure of PCNA3 monomer from Sulfolobus solfataricus.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0006260 | biological_process | DNA replication |
A | 0006272 | biological_process | leading strand elongation |
A | 0006275 | biological_process | regulation of DNA replication |
A | 0030337 | molecular_function | DNA polymerase processivity factor activity |
B | 0003677 | molecular_function | DNA binding |
B | 0006260 | biological_process | DNA replication |
B | 0006272 | biological_process | leading strand elongation |
B | 0006275 | biological_process | regulation of DNA replication |
B | 0030337 | molecular_function | DNA polymerase processivity factor activity |
C | 0003677 | molecular_function | DNA binding |
C | 0006260 | biological_process | DNA replication |
C | 0006272 | biological_process | leading strand elongation |
C | 0006275 | biological_process | regulation of DNA replication |
C | 0030337 | molecular_function | DNA polymerase processivity factor activity |
D | 0003677 | molecular_function | DNA binding |
D | 0006260 | biological_process | DNA replication |
D | 0006272 | biological_process | leading strand elongation |
D | 0006275 | biological_process | regulation of DNA replication |
D | 0030337 | molecular_function | DNA polymerase processivity factor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 601 |
Chain | Residue |
B | SER135 |
B | SER136 |
B | ASP137 |
B | ASP212 |
C | ARG83 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 602 |
Chain | Residue |
C | ARG112 |
C | HOH632 |
C | HOH634 |
A | ASN110 |
C | PHE69 |
C | ASN70 |
C | TYR73 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 603 |
Chain | Residue |
C | SER135 |
C | GLY138 |
C | VAL174 |
C | GLU175 |
C | PHE176 |
C | THR180 |
C | GLY182 |
C | HOH662 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 604 |
Chain | Residue |
A | TYR73 |
A | PHE109 |
A | ASN110 |
C | ASN110 |
C | VAL111 |
C | ARG112 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 605 |
Chain | Residue |
B | SER211 |
B | TYR213 |
B | PHE227 |
B | PHE228 |
B | ASN229 |
B | HOH712 |
B | HOH728 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 606 |
Chain | Residue |
C | THR133 |
C | SER211 |
C | TYR213 |
C | PHE227 |
C | PHE228 |
C | ASN229 |
C | HOH670 |
C | HOH715 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 607 |
Chain | Residue |
B | LYS84 |
B | GLU85 |
B | SER104 |
C | LEU210 |
C | SER211 |
C | ASP212 |
C | ASN229 |
C | GLU231 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 608 |
Chain | Residue |
D | VAL26 |
D | GLU35 |
D | LEU36 |
D | VAL37 |
D | GLU118 |
D | HOH666 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 609 |
Chain | Residue |
A | GLN225 |
A | THR237 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 610 |
Chain | Residue |
D | SER211 |
D | TYR213 |
D | LYS215 |
D | PHE227 |
D | ASN229 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 611 |
Chain | Residue |
B | ARG9 |
B | ARG83 |
B | LYS84 |
C | VAL10 |
C | ASP13 |
C | LYS209 |
C | HOH630 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 612 |
Chain | Residue |
B | ILE102 |
B | HOH751 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO B 613 |
Chain | Residue |
B | PHE109 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 614 |
Chain | Residue |
A | ASN70 |
A | GLN72 |
A | TYR73 |
A | LYS76 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 615 |
Chain | Residue |
B | EDO617 |
C | ARG9 |
C | ARG83 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 616 |
Chain | Residue |
D | VAL80 |
D | ALA81 |
D | LYS82 |
D | ARG83 |
D | GLU85 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 617 |
Chain | Residue |
B | VAL10 |
B | ASP13 |
B | LYS209 |
B | HOH648 |
C | ARG83 |
C | LYS84 |
C | EDO615 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 618 |
Chain | Residue |
C | ILE44 |
C | TYR196 |
C | SER197 |
C | LEU240 |
C | ALA241 |
C | PRO242 |
C | LYS243 |
C | VAL244 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 619 |
Chain | Residue |
D | PHE128 |
D | SER131 |
D | SER189 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 620 |
Chain | Residue |
A | SER131 |
A | GLU187 |
A | LYS215 |
C | LEU126 |
C | GLN127 |
C | PHE128 |
Functional Information from PROSITE/UniProt
site_id | PS01251 |
Number of Residues | 24 |
Details | PCNA_1 Proliferating cell nuclear antigen signature 1. SVeLvALDrAHIsLIsVnLpremF |
Chain | Residue | Details |
A | SER33-PHE56 |