E. coli sliding clamp in complex with AcLF dipeptide. Determined by X-ray diffraction at 1.5 Å resolution. Released 1 May 2013.
Explore 4K3L in 3D Show helices and sheets RCSB PDB PDBe
4K3L contains 29 α-helices and 56 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| α-helix | 7-17 | 11 | |
| α-helix | 29-31 | 3 | |
| β-strand | 32-38 | 7 | 2 |
| β-strand | 41-47 | 7 | 2 |
| β-strand | 51-58 | 8 | 2 |
| β-strand | 64 | 1 | 1 |
| β-strand | 66-71 | 6 | 2 |
| α-helix | 72-81 | 10 | |
| α-helix | 83 | 1 | |
| β-strand | 87-93 | 7 | 1 |
| β-strand | 96-101 | 6 | 1 |
| β-strand | 104-109 | 6 | 1 |
| β-strand | 111 | 1 | 2 |
| α-helix | 113-115 | 3 | |
| α-helix | 119-121 | 3 | |
| β-strand | 126-131 | 6 | 2 |
| α-helix | 132-142 | 11 | |
| α-helix | 143-145 | 3 | |
| α-helix | 153-156 | 4 | |
| β-strand | 158-163 | 6 | 3 |
| β-strand | 166-172 | 7 | 3 |
| β-strand | 176-183 | 8 | 3 |
| β-strand | 191-195 | 5 | 3 |
| α-helix | 197-205 | 9 | |
| β-strand | 213-218 | 6 | 2 |
| β-strand | 222-227 | 6 | 2 |
| β-strand | 230-235 | 6 | 2 |
| α-helix | 244-246 | 3 | |
| β-strand | 254-259 | 6 | 3 |
| α-helix | 260-271 | 12 | |
| β-strand | 280-286 | 7 | 4 |
| β-strand | 289-295 | 7 | 4 |
| β-strand | 301-307 | 7 | 4 |
| β-strand | 309 | 1 | 3 |
| β-strand | 315-320 | 6 | 4 |
| α-helix | 321-331 | 11 | |
| β-strand | 335-340 | 6 | 3 |
| β-strand | 347-351 | 5 | 3 |
| β-strand | 354-361 | 8 | 3 |
| β-strand | 364 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 4 |
| α-helix | 7-17 | 11 | |
| α-helix | 28-31 | 4 | |
| β-strand | 32-38 | 7 | 5 |
| β-strand | 41-47 | 7 | 5 |
| β-strand | 51-58 | 8 | 5 |
| β-strand | 64 | 1 | 4 |
| β-strand | 66-71 | 6 | 5 |
| α-helix | 72-81 | 10 | |
| α-helix | 83 | 1 | |
| β-strand | 87-93 | 7 | 4 |
| β-strand | 96-101 | 6 | 4 |
| β-strand | 104-109 | 6 | 4 |
| β-strand | 111 | 1 | 5 |
| α-helix | 113-115 | 3 | |
| α-helix | 119-121 | 3 | |
| β-strand | 126-130 | 5 | 5 |
| α-helix | 132-142 | 11 | |
| α-helix | 143-145 | 3 | |
| α-helix | 153-155 | 3 | |
| β-strand | 157-163 | 7 | 6 |
| β-strand | 166-172 | 7 | 6 |
| β-strand | 176-183 | 8 | 6 |
| β-strand | 191-196 | 6 | 6 |
| α-helix | 197-206 | 10 | |
| α-helix | 213 | 1 | |
| β-strand | 214-218 | 5 | 5 |
| β-strand | 222-227 | 6 | 5 |
| β-strand | 230-235 | 6 | 5 |
| α-helix | 236-237 | 2 | |
| α-helix | 244-247 | 4 | |
| α-helix | 249 | 1 | |
| β-strand | 254-259 | 6 | 6 |
| α-helix | 260-271 | 12 | |
| β-strand | 280-286 | 7 | 1 |
| β-strand | 289-295 | 7 | 1 |
| β-strand | 301-307 | 7 | 1 |
| β-strand | 309 | 1 | 6 |
| β-strand | 315-320 | 6 | 1 |
| α-helix | 321-331 | 11 | |
| β-strand | 335-340 | 6 | 6 |
| β-strand | 347-351 | 5 | 6 |
| β-strand | 354-361 | 8 | 6 |
| β-strand | 364 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA polymerase III subunit beta | A, B | protein | 366 | Escherichia coli | P0A988 (AlphaFold model) |
>4K3L_1 DNA polymerase III subunit beta (chains A, B) MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGTLSLTGTDLEMEMVARVALV QPHEPGATTVPARKFFDICRGLPEGAEIAVQLEGERMLVRSGRSRFSLSTLPAADFPNLD DWQSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVC SMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGR FPDYRRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQE EAEEILDVTYSGAEMEIGFNVSYVLDVLNALKCENVRMMLTDSVSSVQIEDAASQSAAYV VMPMRL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ACE | Acetyl group | C2 H4 O | 2 |
| CA | Calcium ion | Ca | 12 |
| PHE | Phenylalanine | C9 H11 N O2 | 2 |
| LEU | Leucine | C6 H13 N O2 | 2 |
Water and common crystallization additives (CL, EDO, PGE, PEG) are not listed.
Structural and Thermodynamic Dissection of Linear Motif Recognition by the E. coli Sliding Clamp. Yin, Z., Kelso, M.J., Beck, J.L. et al. J Med Chem (2013) 56:8665-8673. DOI 10.1021/jm401118f · 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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