Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003684 | molecular_function | damaged DNA binding |
A | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006260 | biological_process | DNA replication |
A | 0006261 | biological_process | DNA-templated DNA replication |
A | 0006281 | biological_process | DNA repair |
A | 0006974 | biological_process | DNA damage response |
A | 0042276 | biological_process | error-prone translesion synthesis |
A | 0046872 | molecular_function | metal ion binding |
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 | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 353 |
Chain | Residue |
A | GLU94 |
A | HOH482 |
D | LYS81 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 354 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 355 |
Chain | Residue |
A | GLU120 |
A | GLU127 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 356 |
Chain | Residue |
C | GLY154 |
C | EDO250 |
A | HIS304 |
C | THR151 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 357 |
Chain | Residue |
A | TYR122 |
A | EDO362 |
A | EDO367 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 358 |
Chain | Residue |
A | PHE302 |
A | PRO303 |
A | HIS304 |
A | GLY305 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 359 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 360 |
Chain | Residue |
A | LEU19 |
A | VAL84 |
A | ARG87 |
A | HOH488 |
A | HOH590 |
D | LYS85 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 361 |
Chain | Residue |
A | GLU100 |
A | LYS148 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 362 |
Chain | Residue |
A | VAL165 |
A | ASP167 |
A | EDO357 |
A | HOH631 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 363 |
Chain | Residue |
A | LYS137 |
A | HOH554 |
A | HOH658 |
A | HOH663 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 364 |
Chain | Residue |
A | TYR48 |
A | LYS159 |
C | SER84 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 365 |
Chain | Residue |
A | ARG51 |
A | LYS56 |
A | HOH615 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 366 |
Chain | Residue |
A | ASN130 |
A | ASN161 |
A | HOH451 |
A | HOH559 |
C | GLU140 |
C | ARG213 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 367 |
Chain | Residue |
A | LYS164 |
A | VAL165 |
A | EDO357 |
C | ASN17 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 369 |
Chain | Residue |
A | TYR10 |
A | PRO160 |
A | ASN161 |
A | HOH435 |
C | LYS10 |
site_id | BC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 1PE A 370 |
Chain | Residue |
A | TYR122 |
A | ASN123 |
A | LEU126 |
A | ASN130 |
A | HOH559 |
A | HOH669 |
C | ASN17 |
C | THR20 |
C | ASN21 |
C | ASN144 |
C | LYS206 |
C | LYS210 |
C | ARG213 |
C | HOH475 |
C | HOH573 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 371 |
Chain | Residue |
A | PHE11 |
A | TYR12 |
A | THR45 |
A | ILE104 |
A | ASP105 |
A | HOH595 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 250 |
Chain | Residue |
A | EDO356 |
C | VAL153 |
C | GLU172 |
C | LYS175 |
C | PEG259 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 251 |
Chain | Residue |
C | ARG38 |
C | HIS39 |
C | LEU40 |
C | HOH616 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 252 |
Chain | Residue |
C | LYS54 |
C | TYR60 |
C | ILE62 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 253 |
Chain | Residue |
C | ASN21 |
C | THR41 |
C | LEU46 |
C | ASP207 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 254 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 255 |
Chain | Residue |
C | ILE242 |
C | GLU127 |
C | LYS230 |
C | ASP232 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 256 |
Chain | Residue |
C | THR138 |
C | ASP139 |
C | VAL142 |
C | PRO186 |
C | LEU187 |
C | LYS188 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 257 |
Chain | Residue |
C | MET220 |
C | ASP232 |
C | HIS240 |
C | HOH418 |
site_id | CC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 258 |
Chain | Residue |
C | GLY174 |
C | HOH654 |
D | LYS97 |
D | PRO113 |
site_id | DC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PEG C 259 |
Chain | Residue |
C | LEU152 |
C | VAL153 |
C | LYS175 |
C | ARG176 |
C | EDO250 |
C | HOH382 |
D | ASP78 |
D | GLU111 |
D | HOH546 |
site_id | DC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 260 |
Chain | Residue |
A | LYS282 |
C | GLU156 |
C | ALA170 |
C | GLY171 |
C | GLU172 |
C | HOH495 |
C | HOH607 |
C | HOH618 |
site_id | DC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL C 261 |
Chain | Residue |
A | ALA343 |
C | VAL45 |
C | TYR200 |
C | SER201 |
C | ALA246 |
C | ARG248 |
C | HOH513 |
C | HOH553 |
C | HOH560 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 246 |
Chain | Residue |
D | LEU150 |
D | GLY151 |
D | GLU152 |
D | GLY169 |
D | ASP170 |
D | HOH575 |
site_id | DC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PGE D 247 |
Chain | Residue |
C | LYS175 |
D | GLY70 |
D | PHE71 |
D | LYS72 |
D | ASP75 |
D | LEU112 |
D | PRO113 |
D | HOH392 |
D | HOH598 |
Functional Information from PROSITE/UniProt
site_id | PS01251 |
Number of Residues | 24 |
Details | PCNA_1 Proliferating cell nuclear antigen signature 1. GIrVsGIDpSRVvFLdIfLpssyF |
Chain | Residue | Details |
D | GLY34-PHE57 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | GLU106 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP7 | |
A | ASP105 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Substrate discrimination |
Chain | Residue | Details |
A | TYR12 | |