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

4K3L

E. coli sliding clamp in complex with AcLF dipeptide

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 403
ChainResidue
AGLU6
AHIS9
AGLN61
AHOH560

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ASER181
AGLN355
ASER356

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 405
ChainResidue
AASN295
AASN296
APRO297
AHOH535
AASN275
AARG282

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 406
ChainResidue
AASP121
ATRP122
AARG224
AHOH828

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 408
ChainResidue
AHOH618
AHOH859
BMET1
BLYS2
BGLU64

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
AHOH534
BGLU163
BGLU166
BHOH588
BHOH617
BHOH792

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BPRO249
BPRO252
BMET339
BLEU340
BTHR341
BSER346

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 406
ChainResidue
BGLY46
BGLU202

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 407
ChainResidue
BASP121
BTRP122
BARG224
BHOH651
BHOH836

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B 408
ChainResidue
BALA133
BHOH868

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PGE B 409
ChainResidue
BGLN132
BMET206
BASP208
BGLY210
BASP211
BASN212
BVAL227
BPHE230
BHOH615
BHOH805
BHOH806

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 410
ChainResidue
BSER187
BLEU188
BPRO189
BHOH786
BHOH818

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 412
ChainResidue
APRO65
BVAL126
BGLU127
BHOH616
BHOH790

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 413
ChainResidue
BPRO83
BHOH656

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 414
ChainResidue
BGLU161
BGLU163
BARG168
BASP243
BTYR244
BARG245
BHOH648

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 416
ChainResidue
BGLU95
BTHR110
BHOH688
BHOH817
BHOH822

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 417
ChainResidue
AHOH724
AHOH758
BHOH685
BHOH691
BHOH767
BHOH899

site_idBC9
Number of Residues10
DetailsBINDING SITE FOR LINKED RESIDUES A 400 to 402
ChainResidue
AARG152
ATHR172
AGLY174
AARG176
APRO242
AMET362
AHOH563
AHOH611
AHOH652
BASN251

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR LINKED RESIDUES B 400 to 402
ChainResidue
BMET362
BHOH599
BHOH759
BTHR172
BGLY174
BHIS175
BARG176
BPRO242

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