6FVL
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 |
C | 0003677 | molecular_function | DNA binding |
C | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006260 | biological_process | DNA replication |
C | 0006261 | biological_process | DNA-templated DNA replication |
C | 0006271 | biological_process | DNA strand elongation involved in DNA replication |
C | 0006974 | biological_process | DNA damage response |
C | 0008408 | molecular_function | 3'-5' exonuclease activity |
C | 0009360 | cellular_component | DNA polymerase III complex |
C | 0030174 | biological_process | regulation of DNA-templated DNA replication initiation |
C | 0030894 | cellular_component | replisome |
C | 0032297 | biological_process | negative regulation of DNA-templated DNA replication initiation |
C | 0042276 | biological_process | error-prone translesion synthesis |
C | 0042802 | molecular_function | identical protein binding |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0044787 | biological_process | bacterial-type DNA replication |
C | 1990078 | cellular_component | replication inhibiting complex |
C | 1990085 | cellular_component | Hda-beta clamp complex |
D | 0003677 | molecular_function | DNA binding |
D | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006260 | biological_process | DNA replication |
D | 0006261 | biological_process | DNA-templated DNA replication |
D | 0006271 | biological_process | DNA strand elongation involved in DNA replication |
D | 0006974 | biological_process | DNA damage response |
D | 0008408 | molecular_function | 3'-5' exonuclease activity |
D | 0009360 | cellular_component | DNA polymerase III complex |
D | 0030174 | biological_process | regulation of DNA-templated DNA replication initiation |
D | 0030894 | cellular_component | replisome |
D | 0032297 | biological_process | negative regulation of DNA-templated DNA replication initiation |
D | 0042276 | biological_process | error-prone translesion synthesis |
D | 0042802 | molecular_function | identical protein binding |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0044787 | biological_process | bacterial-type DNA replication |
D | 1990078 | cellular_component | replication inhibiting complex |
D | 1990085 | cellular_component | Hda-beta clamp complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue 1PE A 401 |
Chain | Residue |
A | GLN15 |
A | SER18 |
A | GLY22 |
A | ARG73 |
A | PHE76 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue 1PE A 402 |
Chain | Residue |
A | ARG279 |
B | ASP77 |
A | ALA271 |
A | ILE272 |
A | SER274 |
A | GLU276 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue 1PE A 403 |
Chain | Residue |
A | ALA58 |
A | ASP229 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | ARG365 |
C | ARG152 |
J | PHE6 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | ASN295 |
A | HOH546 |
A | HOH577 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue 1PE B 401 |
Chain | Residue |
B | SER18 |
B | ARG73 |
B | PHE76 |
B | HOH565 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue 1PE B 402 |
Chain | Residue |
B | GLU140 |
B | ASN329 |
B | ALA330 |
B | LYS332 |
B | 1PE406 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue 1PE B 403 |
Chain | Residue |
B | GLN149 |
B | ASP150 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue 1PE B 404 |
Chain | Residue |
B | GLU161 |
B | GLU163 |
B | SER192 |
B | ARG245 |
B | HOH528 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue 1PE B 405 |
Chain | Residue |
B | PRO213 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue 1PE B 406 |
Chain | Residue |
B | ARG137 |
B | 1PE402 |
D | ASP211 |
D | ASN212 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue 1PE B 407 |
Chain | Residue |
B | HIS9 |
B | ARG56 |
B | ALA58 |
B | VAL60 |
B | ASP229 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue GOL B 408 |
Chain | Residue |
B | SER-1 |
B | ALA67 |
B | THR68 |
B | LEU92 |
B | GLY94 |
B | GLU95 |
B | ALA113 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue GOL B 409 |
Chain | Residue |
B | ARG282 |
B | ASN295 |
B | LEU366 |
B | HOH502 |
B | HOH516 |
B | HOH574 |
site_id | AD6 |
Number of Residues | 10 |
Details | binding site for residue 1PE C 401 |
Chain | Residue |
A | ASP307 |
A | VAL308 |
A | THR309 |
A | GLU334 |
A | ASN335 |
C | GLU257 |
C | ALA258 |
C | VAL308 |
C | THR309 |
C | ASN335 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue 1PE C 402 |
Chain | Residue |
C | PRO83 |
C | SER101 |
C | GLY102 |
C | ARG103 |
C | SER104 |
D | ARG269 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue 1PE C 403 |
Chain | Residue |
C | SER18 |
C | GLY22 |
C | ARG73 |
C | PHE76 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue 1PE D 401 |
Chain | Residue |
D | TYR154 |
D | ARG240 |
D | PRO242 |
D | ASP243 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue 1PE D 402 |
Chain | Residue |
D | ARG7 |
D | ARG80 |
D | GLY81 |
D | LEU82 |
site_id | AE2 |
Number of Residues | 3 |
Details | binding site for residue GOL D 403 |
Chain | Residue |
D | ASN295 |
D | LEU366 |
D | HOH509 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue GOL H 101 |
Chain | Residue |
C | HIS175 |
H | ASP4 |
J | GLN2 |
J | ASP4 |
site_id | AE4 |
Number of Residues | 7 |
Details | binding site for residue 1PE I 101 |
Chain | Residue |
I | ASP4 |
B | ARG365 |
D | TYR153 |
D | TYR154 |
D | GLY239 |
D | ARG240 |
I | GLN2 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue GOL I 102 |
Chain | Residue |
B | ARG152 |
D | ARG152 |
I | PHE6 |
K | PHE6 |
site_id | AE6 |
Number of Residues | 8 |
Details | binding site for residue 1PE K 101 |
Chain | Residue |
B | TYR153 |
B | TYR154 |
B | GLY239 |
B | ARG240 |
D | VAL344 |
K | GLN2 |
K | ALC3 |
K | ASP4 |
site_id | AE7 |
Number of Residues | 9 |
Details | binding site for Di-peptide ACE H 1 and GLN H 2 |
Chain | Residue |
A | HIS175 |
A | TYR323 |
A | MET362 |
A | PRO363 |
A | MET364 |
A | ARG365 |
C | VAL151 |
H | ALC3 |
H | HOH201 |
site_id | AE8 |
Number of Residues | 9 |
Details | binding site for Di-peptide GLN H 2 and ALC H 3 |
Chain | Residue |
A | HIS175 |
A | TYR323 |
A | MET362 |
A | PRO363 |
A | MET364 |
A | ARG365 |
H | ACE1 |
H | ASP4 |
H | HOH201 |
site_id | AE9 |
Number of Residues | 11 |
Details | binding site for Di-peptide ALC H 3 and ASP H 4 |
Chain | Residue |
A | GLY174 |
A | HIS175 |
A | MET362 |
A | PRO363 |
A | ARG365 |
H | ACE1 |
H | GLN2 |
H | LEU5 |
H | PHE6 |
H | GOL101 |
H | HOH202 |
site_id | AF1 |
Number of Residues | 12 |
Details | binding site for Di-peptide ACE I 1 and GLN I 2 |
Chain | Residue |
B | HIS175 |
B | TYR323 |
B | MET362 |
B | PRO363 |
B | MET364 |
B | ARG365 |
D | TYR153 |
I | ALC3 |
I | 1PE101 |
I | HOH201 |
I | HOH202 |
I | HOH203 |
site_id | AF2 |
Number of Residues | 14 |
Details | binding site for Di-peptide GLN I 2 and ALC I 3 |
Chain | Residue |
B | HIS175 |
B | TYR323 |
B | MET362 |
B | PRO363 |
B | MET364 |
B | ARG365 |
D | TYR153 |
D | ARG240 |
I | ACE1 |
I | ASP4 |
I | 1PE101 |
I | HOH201 |
I | HOH202 |
I | HOH203 |
site_id | AF3 |
Number of Residues | 15 |
Details | binding site for Di-peptide ALC I 3 and ASP I 4 |
Chain | Residue |
B | GLY174 |
B | HIS175 |
B | MET362 |
B | PRO363 |
B | ARG365 |
B | HOH564 |
D | ARG152 |
D | TYR154 |
D | ARG240 |
I | ACE1 |
I | GLN2 |
I | LEU5 |
I | PHE6 |
I | 1PE101 |
I | HOH201 |
site_id | AF4 |
Number of Residues | 10 |
Details | binding site for Di-peptide ACE J 1 and GLN J 2 |
Chain | Residue |
A | VAL151 |
C | HIS175 |
C | MET362 |
C | PRO363 |
C | MET364 |
C | ARG365 |
H | GOL101 |
J | ALC3 |
J | HOH101 |
J | HOH102 |
site_id | AF5 |
Number of Residues | 10 |
Details | binding site for Di-peptide GLN J 2 and ALC J 3 |
Chain | Residue |
C | HIS175 |
C | VAL344 |
C | MET362 |
C | PRO363 |
C | MET364 |
H | GOL101 |
J | ACE1 |
J | ASP4 |
J | HOH101 |
J | HOH102 |
site_id | AF6 |
Number of Residues | 10 |
Details | binding site for Di-peptide ALC J 3 and ASP J 4 |
Chain | Residue |
C | GLY174 |
C | HIS175 |
C | VAL344 |
C | MET362 |
C | PRO363 |
H | GOL101 |
J | ACE1 |
J | GLN2 |
J | LEU5 |
J | PHE6 |
site_id | AF7 |
Number of Residues | 11 |
Details | binding site for Di-peptide ACE K 1 and GLN K 2 |
Chain | Residue |
B | TYR153 |
D | HIS175 |
D | MET362 |
D | PRO363 |
D | MET364 |
D | ARG365 |
D | HOH513 |
K | ALC3 |
K | 1PE101 |
K | HOH201 |
K | HOH202 |
site_id | AF8 |
Number of Residues | 12 |
Details | binding site for Di-peptide GLN K 2 and ALC K 3 |
Chain | Residue |
B | TYR153 |
B | ARG240 |
D | HIS175 |
D | MET362 |
D | PRO363 |
D | MET364 |
D | HOH513 |
K | ACE1 |
K | ASP4 |
K | 1PE101 |
K | HOH201 |
K | HOH202 |
site_id | AF9 |
Number of Residues | 11 |
Details | binding site for Di-peptide ALC K 3 and ASP K 4 |
Chain | Residue |
B | TYR154 |
B | ARG240 |
D | HIS175 |
D | MET362 |
D | PRO363 |
D | HOH513 |
K | ACE1 |
K | GLN2 |
K | LEU5 |
K | PHE6 |
K | 1PE101 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:18191219 |
Chain | Residue | Details |
A | ARG24 | |
D | ARG24 | |
D | GLN149 | |
D | TYR153 | |
A | GLN149 | |
A | TYR153 | |
B | ARG24 | |
B | GLN149 | |
B | TYR153 | |
C | ARG24 | |
C | GLN149 | |
C | TYR153 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18191219 |
Chain | Residue | Details |
A | ARG73 | |
B | ARG73 | |
C | ARG73 | |
D | ARG73 |