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

4K3M

E.coli sliding clamp in complex with AcALDLF 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 Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 401
ChainResidue
AALA86
AGLU87
AALA89
AARG100
ASER101
AGLY102
AHOH596

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
ASER107
AHOH707

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AGLY280
AALA294
AASN295
AHOH573

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE A 404
ChainResidue
AHIS9
ATHR41
AARG56
AVAL57
AALA58
AASP229

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 405
ChainResidue
ASER181

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASP211

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BGLU161
BTHR162
BSER190
BHIS191
BHOH736

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BGLU84
BHOH767
BHOH806

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 B 404
ChainResidue
AALA38
BASP121
BTRP122
BGLN217
BARG224

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 405
ChainResidue
BVAL17
BGLY46
BASP48
BMET51
BGLU202

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE B 406
ChainResidue
BTYR284
BLYS291
BHOH745
BHOH747
BHOH753

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG B 407
ChainResidue
ALYS74
AASP77
BALA271
BILE272
BSER274
BGLU276
BARG279
BHOH687
BHOH760

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 408
ChainResidue
AHOH760
BGLU163
BHOH814
BHOH823

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon