6FVM
Mutant DNA polymerase sliding clamp from Escherichia coli with bound P7 peptide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006260 | biological_process | DNA replication |
A | 0006261 | biological_process | DNA-templated DNA replication |
A | 0006271 | biological_process | DNA strand elongation involved in DNA replication |
A | 0006974 | biological_process | DNA damage response |
A | 0008408 | molecular_function | 3'-5' exonuclease activity |
A | 0009360 | cellular_component | DNA polymerase III complex |
A | 0030174 | biological_process | regulation of DNA-templated DNA replication initiation |
A | 0030894 | cellular_component | replisome |
A | 0032297 | biological_process | negative regulation of DNA-templated DNA replication initiation |
A | 0042276 | biological_process | error-prone translesion synthesis |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0044787 | biological_process | bacterial-type DNA replication |
A | 1990078 | cellular_component | replication inhibiting complex |
A | 1990085 | cellular_component | Hda-beta clamp complex |
B | 0003677 | molecular_function | DNA binding |
B | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006260 | biological_process | DNA replication |
B | 0006261 | biological_process | DNA-templated DNA replication |
B | 0006271 | biological_process | DNA strand elongation involved in DNA replication |
B | 0006974 | biological_process | DNA damage response |
B | 0008408 | molecular_function | 3'-5' exonuclease activity |
B | 0009360 | cellular_component | DNA polymerase III complex |
B | 0030174 | biological_process | regulation of DNA-templated DNA replication initiation |
B | 0030894 | cellular_component | replisome |
B | 0032297 | biological_process | negative regulation of DNA-templated DNA replication initiation |
B | 0042276 | biological_process | error-prone translesion synthesis |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0044787 | biological_process | bacterial-type DNA replication |
B | 1990078 | cellular_component | replication inhibiting complex |
B | 1990085 | cellular_component | Hda-beta clamp complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 401 |
Chain | Residue |
A | GLU6 |
A | HIS9 |
A | GLN61 |
A | HOH542 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue 1PE A 402 |
Chain | Residue |
A | ARG80 |
A | LEU82 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue 1PE A 403 |
Chain | Residue |
A | ALA58 |
A | VAL60 |
A | ASP229 |
A | HIS9 |
A | PRO28 |
A | ARG56 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue 1PE A 404 |
Chain | Residue |
A | SER18 |
A | LEU21 |
A | GLY22 |
A | ARG73 |
A | PHE76 |
A | HOH605 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue 1PE A 405 |
Chain | Residue |
A | TYR284 |
A | LYS291 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 406 |
Chain | Residue |
A | SER192 |
A | ILE194 |
A | GLY239 |
A | PHE241 |
A | HOH525 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue 1PE B 401 |
Chain | Residue |
B | SER18 |
B | LEU21 |
B | GLY23 |
B | ARG73 |
B | PHE76 |
B | ARG80 |
B | HOH505 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue 1PE B 402 |
Chain | Residue |
B | GLU161 |
B | SER190 |
B | ARG245 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue 1PE B 403 |
Chain | Residue |
B | HIS9 |
B | ARG56 |
B | ALA58 |
B | VAL60 |
B | ASP229 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue 1PE B 404 |
Chain | Residue |
A | PRO297 |
A | HOH672 |
B | PRO83 |
B | GLU84 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue 1PE B 405 |
Chain | Residue |
B | SER192 |
B | GLY239 |
B | ARG240 |
B | PHE241 |
B | PRO242 |
B | ASP243 |
B | HOH512 |
B | HOH562 |
site_id | AD3 |
Number of Residues | 13 |
Details | binding site for Di-peptide ACE H 1 and GLN H 2 |
Chain | Residue |
A | HIS175 |
A | TYR323 |
A | GLU334 |
A | ASN335 |
A | ALA353 |
A | MET362 |
A | PRO363 |
A | MET364 |
A | ARG365 |
A | HOH501 |
A | HOH520 |
A | HOH555 |
H | ALC3 |
site_id | AD4 |
Number of Residues | 12 |
Details | binding site for Di-peptide GLN H 2 and ALC H 3 |
Chain | Residue |
A | HIS175 |
A | TYR323 |
A | ALA353 |
A | MET362 |
A | PRO363 |
A | MET364 |
A | ARG365 |
A | HOH501 |
A | HOH520 |
A | HOH555 |
H | ACE1 |
H | ASP4 |
site_id | AD5 |
Number of Residues | 11 |
Details | binding site for Di-peptide ALC H 3 and ASP H 4 |
Chain | Residue |
A | GLY174 |
A | HIS175 |
A | ALA353 |
A | MET362 |
A | PRO363 |
A | ARG365 |
H | ACE1 |
H | GLN2 |
H | LEU5 |
H | PHE6 |
H | HOH101 |
site_id | AD6 |
Number of Residues | 13 |
Details | binding site for Di-peptide ACE I 1 and GLN I 2 |
Chain | Residue |
I | HOH105 |
I | HOH106 |
B | HIS175 |
B | TYR323 |
B | GLU334 |
B | ASN335 |
B | MET362 |
B | PRO363 |
B | MET364 |
B | ARG365 |
I | ALC3 |
I | HOH102 |
I | HOH103 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for Di-peptide GLN I 2 and ALC I 3 |
Chain | Residue |
B | HIS175 |
B | TYR323 |
B | GLU334 |
B | ASN335 |
B | MET362 |
B | PRO363 |
B | MET364 |
B | ARG365 |
I | ACE1 |
I | ASP4 |
I | HOH102 |
I | HOH103 |
I | HOH105 |
I | HOH106 |
site_id | AD8 |
Number of Residues | 12 |
Details | binding site for Di-peptide ALC I 3 and ASP I 4 |
Chain | Residue |
B | GLU334 |
B | ASN335 |
B | MET362 |
B | PRO363 |
B | ARG365 |
B | HOH580 |
I | ACE1 |
I | GLN2 |
I | LEU5 |
I | PHE6 |
I | HOH104 |
I | HOH107 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:18191219 |
Chain | Residue | Details |
A | ARG24 | |
A | GLN149 | |
A | TYR153 | |
B | ARG24 | |
B | GLN149 | |
B | TYR153 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18191219 |
Chain | Residue | Details |
A | ARG73 | |
B | ARG73 |