Nucleotide bound form of an isolated E. coli clamp loader gamma subunit. Determined by X-ray diffraction at 2.3 Å resolution. Released 8 Apr 2003.
Explore 1NJF in 3D Show helices and sheets RCSB PDB PDBe
1NJF contains 60 α-helices and 28 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 6-9 | 4 | |
| α-helix | 15-17 | 3 | |
| α-helix | 22-33 | 12 | |
| β-strand | 40-44 | 5 | 1 |
| α-helix | 51-63 | 13 | |
| α-helix | 77-84 | 8 | |
| β-strand | 90-94 | 5 | 1 |
| α-helix | 101-109 | 9 | |
| β-strand | 121-126 | 6 | 1 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 1 |
| α-helix | 159-161 | 3 | |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 1 |
| α-helix | 175-179 | 5 | |
| α-helix | 180-194 | 15 | |
| β-strand | 198 | 1 | 2 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-227 | 14 | |
| β-strand | 232 | 1 | 2 |
| α-helix | 234-241 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-9 | 4 | |
| α-helix | 15-17 | 3 | |
| α-helix | 22-34 | 13 | |
| β-strand | 40-44 | 5 | 5 |
| α-helix | 51-63 | 13 | |
| α-helix | 77-83 | 7 | |
| β-strand | 90-94 | 5 | 5 |
| α-helix | 102-109 | 8 | |
| β-strand | 121-126 | 6 | 5 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 5 |
| α-helix | 159-161 | 3 | |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 5 |
| α-helix | 175-179 | 5 | |
| α-helix | 180-194 | 15 | |
| β-strand | 198 | 1 | 6 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-227 | 14 | |
| β-strand | 232 | 1 | 6 |
| α-helix | 234-241 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-9 | 4 | |
| α-helix | 15-17 | 3 | |
| α-helix | 22-33 | 12 | |
| β-strand | 40-44 | 5 | 7 |
| α-helix | 51-63 | 13 | |
| α-helix | 77-83 | 7 | |
| β-strand | 90-94 | 5 | 7 |
| α-helix | 101-109 | 9 | |
| β-strand | 121-126 | 6 | 7 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 7 |
| α-helix | 159-161 | 3 | |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 7 |
| α-helix | 175-179 | 5 | |
| α-helix | 180-194 | 15 | |
| β-strand | 198 | 1 | 8 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-227 | 14 | |
| β-strand | 232 | 1 | 8 |
| α-helix | 234-241 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA polymerase III subunit gamma | A, B, C, D | protein | 250 | Escherichia coli | P06710 (AlphaFold model) |
>1NJF_1 DNA polymerase III subunit gamma (chains A, B, C, D) GAHMGGSMSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTS IARLLAKGLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQY APARGRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQF HLKALDVEQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVS TQAVSAMLGT
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| AGS | Phosphothiophosphoric acid-adenylate ester | C10 H16 N5 O12 P3 S | 3 |
| ZN | Zinc ion | Zn | 4 |
Nucleotide-Induced Conformational Changes in an Isolated Escherichia coli DNA Polymerase III Clamp Loader Subunit. Podobnik, M., Weitze, T.F., O'Donnell, M. et al. Structure (2003) 11:253-263. DOI 10.1016/S0969-2126(03)00027-3 · PubMed
Other PDB entries of the same protein (UniProt P06710 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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