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6FVM

Mutant DNA polymerase sliding clamp from Escherichia coli with bound P7 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006260biological_processDNA replication
A0006261biological_processDNA-templated DNA replication
A0006271biological_processDNA strand elongation involved in DNA replication
A0006974biological_processDNA damage response
A0008408molecular_function3'-5' exonuclease activity
A0009360cellular_componentDNA polymerase III complex
A0030174biological_processregulation of DNA-templated DNA replication initiation
A0030894cellular_componentreplisome
A0032297biological_processnegative regulation of DNA-templated DNA replication initiation
A0042276biological_processerror-prone translesion synthesis
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0044787biological_processbacterial-type DNA replication
A1990078cellular_componentreplication inhibiting complex
A1990085cellular_componentHda-beta clamp complex
B0003677molecular_functionDNA binding
B0003887molecular_functionDNA-directed DNA polymerase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006260biological_processDNA replication
B0006261biological_processDNA-templated DNA replication
B0006271biological_processDNA strand elongation involved in DNA replication
B0006974biological_processDNA damage response
B0008408molecular_function3'-5' exonuclease activity
B0009360cellular_componentDNA polymerase III complex
B0030174biological_processregulation of DNA-templated DNA replication initiation
B0030894cellular_componentreplisome
B0032297biological_processnegative regulation of DNA-templated DNA replication initiation
B0042276biological_processerror-prone translesion synthesis
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0044787biological_processbacterial-type DNA replication
B1990078cellular_componentreplication inhibiting complex
B1990085cellular_componentHda-beta clamp complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 401
ChainResidue
AGLU6
AHIS9
AGLN61
AHOH542

site_idAC2
Number of Residues2
Detailsbinding site for residue 1PE A 402
ChainResidue
AARG80
ALEU82

site_idAC3
Number of Residues6
Detailsbinding site for residue 1PE A 403
ChainResidue
AALA58
AVAL60
AASP229
AHIS9
APRO28
AARG56

site_idAC4
Number of Residues6
Detailsbinding site for residue 1PE A 404
ChainResidue
ASER18
ALEU21
AGLY22
AARG73
APHE76
AHOH605

site_idAC5
Number of Residues2
Detailsbinding site for residue 1PE A 405
ChainResidue
ATYR284
ALYS291

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 406
ChainResidue
ASER192
AILE194
AGLY239
APHE241
AHOH525

site_idAC7
Number of Residues7
Detailsbinding site for residue 1PE B 401
ChainResidue
BSER18
BLEU21
BGLY23
BARG73
BPHE76
BARG80
BHOH505

site_idAC8
Number of Residues3
Detailsbinding site for residue 1PE B 402
ChainResidue
BGLU161
BSER190
BARG245

site_idAC9
Number of Residues5
Detailsbinding site for residue 1PE B 403
ChainResidue
BHIS9
BARG56
BALA58
BVAL60
BASP229

site_idAD1
Number of Residues4
Detailsbinding site for residue 1PE B 404
ChainResidue
APRO297
AHOH672
BPRO83
BGLU84

site_idAD2
Number of Residues8
Detailsbinding site for residue 1PE B 405
ChainResidue
BSER192
BGLY239
BARG240
BPHE241
BPRO242
BASP243
BHOH512
BHOH562

site_idAD3
Number of Residues13
Detailsbinding site for Di-peptide ACE H 1 and GLN H 2
ChainResidue
AHIS175
ATYR323
AGLU334
AASN335
AALA353
AMET362
APRO363
AMET364
AARG365
AHOH501
AHOH520
AHOH555
HALC3

site_idAD4
Number of Residues12
Detailsbinding site for Di-peptide GLN H 2 and ALC H 3
ChainResidue
AHIS175
ATYR323
AALA353
AMET362
APRO363
AMET364
AARG365
AHOH501
AHOH520
AHOH555
HACE1
HASP4

site_idAD5
Number of Residues11
Detailsbinding site for Di-peptide ALC H 3 and ASP H 4
ChainResidue
AGLY174
AHIS175
AALA353
AMET362
APRO363
AARG365
HACE1
HGLN2
HLEU5
HPHE6
HHOH101

site_idAD6
Number of Residues13
Detailsbinding site for Di-peptide ACE I 1 and GLN I 2
ChainResidue
IHOH105
IHOH106
BHIS175
BTYR323
BGLU334
BASN335
BMET362
BPRO363
BMET364
BARG365
IALC3
IHOH102
IHOH103

site_idAD7
Number of Residues14
Detailsbinding site for Di-peptide GLN I 2 and ALC I 3
ChainResidue
BHIS175
BTYR323
BGLU334
BASN335
BMET362
BPRO363
BMET364
BARG365
IACE1
IASP4
IHOH102
IHOH103
IHOH105
IHOH106

site_idAD8
Number of Residues12
Detailsbinding site for Di-peptide ALC I 3 and ASP I 4
ChainResidue
BGLU334
BASN335
BMET362
BPRO363
BARG365
BHOH580
IACE1
IGLN2
ILEU5
IPHE6
IHOH104
IHOH107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:18191219
ChainResidueDetails
AARG24
AGLN149
ATYR153
BARG24
BGLN149
BTYR153

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18191219
ChainResidueDetails
AARG73
BARG73

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PDB entries from 2024-10-09

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