4MJR: E. coli sliding clamp

E. coli sliding clamp in complex with (S)-Carprofen. Determined by X-ray diffraction at 1.62 Å resolution. Released 18 Sept 2013.

Method
X-ray diffraction
Resolution
1.62 Å
Organism
Escherichia coli
Chains
2
Atoms
6,404
Mol. weight
82.41 kDa
Ligands
CA, 0LA
Released
18 Sept 2013

Explore 4MJR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MJR contains 29 α-helices and 53 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 14 helices, 26 β-strands

ElementResiduesLengthSheet
β-strand2-651
α-helix7-1711
α-helix28-314
β-strand32-3872
β-strand41-4772
β-strand51-5882
β-strand6411
β-strand66-7162
α-helix72-8110
α-helix831
β-strand87-9371
β-strand96-10161
β-strand104-10961
β-strand11112
α-helix113-1153
α-helix119-1213
β-strand124-13182
α-helix132-14211
α-helix143-1453
α-helix153-1553
β-strand157-172163
β-strand176-196213
α-helix197-20610
β-strand213-21972
β-strand222-22762
β-strand230-23562
α-helix2361
β-strand23713
α-helix244-2463
β-strand254-25963
α-helix260-27112
β-strand280-28674
β-strand289-29574
β-strand301-30774
β-strand309-31133
β-strand315-32064
α-helix321-33111
β-strand335-34063
β-strand347-35153
β-strand357-36153
Chain B: 15 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand2-654
α-helix7-1711
α-helix28-314
β-strand32-3875
β-strand41-4775
β-strand51-5885
β-strand6414
β-strand66-7165
α-helix72-8110
α-helix831
β-strand87-9374
β-strand96-10164
β-strand104-10964
β-strand11115
α-helix113-1153
α-helix119-1213
β-strand126-13055
α-helix132-1409
α-helix143-1453
α-helix153-1553
β-strand157-172166
β-strand176-196216
α-helix197-2059
α-helix212-2132
β-strand214-21855
β-strand222-22765
β-strand230-23565
α-helix2361
β-strand23716
α-helix244-2463
β-strand254-25966
α-helix260-27112
β-strand280-28671
β-strand289-29571
β-strand301-30771
β-strand309-31026
β-strand315-32061
α-helix321-33111
β-strand335-34066
β-strand347-35156
β-strand357-36156
β-strand36411

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA polymerase III subunit betaA, Bprotein366Escherichia coliP0A988 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4MJR_1 DNA polymerase III subunit beta (chains A, B)
MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGTLSLTGTDLEMEMVARVALV
QPHEPGATTVPARKFFDICRGLPEGAEIAVQLEGERMLVRSGRSRFSLSTLPAADFPNLD
DWQSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVC
SMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGR
FPDYRRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQE
EAEEILDVTYSGAEMEIGFNVSYVLDVLNALKCENVRMMLTDSVSSVQIEDAASQSAAYV
VMPMRL

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1
0LA(2S)-2-(6-chloro-9H-carbazol-2-yl)propanoic acidC15 H12 Cl N O21

Water and common crystallization additives (CL, PEG, PGE) are not listed.

Primary citation

DNA replication is the target for the antibacterial effects of nonsteroidal anti-inflammatory drugs. Yin, Z., Wang, Y., Whittell, L.R. et al. Chem Biol (2014) 21:481-487. DOI 10.1016/j.chembiol.2014.02.009 · PubMed

Other PDB entries of the same protein (UniProt P0A988 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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