Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6E8E

Crystal structure of the Escherichia coli sliding clamp-MutL complex.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006260biological_processDNA replication
A0006261biological_processDNA-templated DNA replication
A0006271biological_processDNA strand elongation involved in DNA replication
A0006298biological_processmismatch repair
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
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006260biological_processDNA replication
B0006261biological_processDNA-templated DNA replication
B0006271biological_processDNA strand elongation involved in DNA replication
B0006298biological_processmismatch repair
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 Residues5
Detailsbinding site for residue GOL A 601
ChainResidue
AARG206
ASER219
ATYR282
AGLN393
ASER394

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 602
ChainResidue
AGLN187
AASN194
AARG235

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 603
ChainResidue
BTRP160
BGLN161
BSER258
BASN259
BASN260
ATYR191

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 604
ChainResidue
AARG190
AGLY212
AILE434
AHOH711
AHOH773

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 605
ChainResidue
AGLN224
ASER225
AHOH727
BGLY140
BARG141

site_idAC6
Number of Residues9
Detailsbinding site for residue SO4 A 606
ChainResidue
AHIS213
AASN358
ATYR361
AMET402
ALEU476
AARG479
AGLN480
AHOH708
AHOH732

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 A 607
ChainResidue
APRO287
ALYS288
ASER384

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 601
ChainResidue
BGLN187
BASN194
BARG235
BHOH749

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL B 602
ChainResidue
BARG190
BGLY212
BILE434
BLEU436
BHOH754

site_idAD1
Number of Residues7
Detailsbinding site for residue SO4 B 603
ChainResidue
BASN358
BTYR361
BLEU476
BARG479
BGLN480
BHOH706
BHOH759

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 B 604
ChainResidue
BPRO477
BHOH719
BHOH762

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:18191219
ChainResidueDetails
BARG62
BGLN187
BTYR191

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18191219
ChainResidueDetails
BARG111

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon