Crystal Structure of the Processivity Clamp Loader Gamma Complex of E. coli DNA Polymerase III. Determined by X-ray diffraction at 2.7 Å resolution. Released 26 Sept 2001.
Explore 1JR3 in 3D Show helices and sheets RCSB PDB PDBe
1JR3 contains 104 α-helices and 39 β-strands across 5 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 | 22-34 | 13 | |
| β-strand | 40-44 | 5 | 1 |
| α-helix | 51-62 | 12 | |
| α-helix | 77-83 | 7 | |
| β-strand | 91-94 | 4 | 1 |
| α-helix | 104-110 | 7 | |
| α-helix | 114-115 | 2 | |
| 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 | 176-179 | 4 | |
| 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 | 234-240 | 7 | |
| α-helix | 246-258 | 13 | |
| α-helix | 261-273 | 13 | |
| α-helix | 278-295 | 18 | |
| α-helix | 305-308 | 4 | |
| α-helix | 310-319 | 10 | |
| α-helix | 322-338 | 17 | |
| α-helix | 345-358 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2015-2017 | 3 | |
| α-helix | 2022-2034 | 13 | |
| β-strand | 2040-2044 | 5 | 3 |
| α-helix | 2051-2063 | 13 | |
| α-helix | 77-84 | 8 | |
| β-strand | 91-94 | 4 | 3 |
| α-helix | 104-107 | 4 | |
| α-helix | 114-115 | 2 | |
| β-strand | 121-126 | 6 | 3 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-143 | 11 | |
| β-strand | 150-155 | 6 | 3 |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 3 |
| α-helix | 175-176 | 2 | |
| α-helix | 180-193 | 14 | |
| β-strand | 197-198 | 2 | 4 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-227 | 14 | |
| β-strand | 231-232 | 2 | 4 |
| α-helix | 234-240 | 7 | |
| α-helix | 248-256 | 9 | |
| α-helix | 262-273 | 12 | |
| α-helix | 278-297 | 20 | |
| α-helix | 305-308 | 4 | |
| α-helix | 310-319 | 10 | |
| α-helix | 322-338 | 17 | |
| α-helix | 345-358 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-9 | 4 | |
| α-helix | 5015-5017 | 3 | |
| α-helix | 22-34 | 13 | |
| β-strand | 40-44 | 5 | 5 |
| β-strand | 47 | 1 | 6 |
| β-strand | 49 | 1 | 6 |
| α-helix | 51-63 | 13 | |
| α-helix | 77-84 | 8 | |
| β-strand | 90-94 | 5 | 5 |
| α-helix | 104-109 | 6 | |
| α-helix | 110-112 | 3 | |
| α-helix | 114-115 | 2 | |
| β-strand | 121-126 | 6 | 5 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 5 |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 5 |
| α-helix | 176-179 | 4 | |
| α-helix | 180-194 | 15 | |
| β-strand | 198 | 1 | 7 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-228 | 15 | |
| β-strand | 232 | 1 | 7 |
| α-helix | 234-237 | 4 | |
| α-helix | 251-257 | 7 | |
| α-helix | 261-273 | 13 | |
| α-helix | 278-294 | 17 | |
| α-helix | 299-301 | 3 | |
| α-helix | 310-319 | 10 | |
| α-helix | 322-338 | 17 | |
| α-helix | 339-341 | 3 | |
| α-helix | 345-358 | 14 | |
| α-helix | 364-366 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 8 |
| α-helix | 9-15 | 7 | |
| β-strand | 20-25 | 6 | 8 |
| α-helix | 28-45 | 18 | |
| β-strand | 49-54 | 6 | 8 |
| α-helix | 61-73 | 13 | |
| β-strand | 78-83 | 6 | 8 |
| α-helix | 93-101 | 9 | |
| β-strand | 105 | 1 | 8 |
| β-strand | 108-114 | 7 | 8 |
| α-helix | 116-118 | 3 | |
| α-helix | 125-130 | 6 | |
| β-strand | 135-139 | 5 | 8 |
| α-helix | 141-143 | 3 | |
| α-helix | 146-157 | 12 | |
| β-strand | 161-162 | 2 | 9 |
| α-helix | 164-172 | 9 | |
| α-helix | 178-191 | 14 | |
| β-strand | 196-197 | 2 | 9 |
| α-helix | 199-209 | 11 | |
| α-helix | 214-221 | 8 | |
| α-helix | 226-233 | 8 | |
| α-helix | 243-261 | 19 | |
| α-helix | 269-276 | 8 | |
| α-helix | 282-292 | 11 | |
| α-helix | 295-314 | 20 | |
| α-helix | 320-330 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-15 | 9 | |
| β-strand | 26-30 | 5 | 10 |
| α-helix | 37-48 | 12 | |
| α-helix | 63-69 | 7 | |
| β-strand | 76-79 | 4 | 10 |
| α-helix | 80-82 | 3 | |
| β-strand | 88 | 1 | 11 |
| α-helix | 90-100 | 11 | |
| β-strand | 110-114 | 5 | 10 |
| α-helix | 117-119 | 3 | |
| β-strand | 120 | 1 | 11 |
| α-helix | 122-133 | 12 | |
| β-strand | 139-145 | 7 | 10 |
| β-strand | 160-163 | 4 | 10 |
| α-helix | 165-168 | 4 | |
| α-helix | 169-179 | 11 | |
| α-helix | 184-192 | 9 | |
| α-helix | 198-205 | 8 | |
| α-helix | 209-226 | 18 | |
| α-helix | 229-232 | 4 | |
| α-helix | 233-236 | 4 | |
| α-helix | 241-259 | 19 | |
| α-helix | 271-280 | 10 | |
| α-helix | 283-301 | 19 | |
| α-helix | 308-322 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA polymerase III subunit gamma | A, B, C | protein | 373 | Escherichia coli | P06710 (AlphaFold model) |
| DNA polymerase III, delta subunit | D | protein | 343 | Escherichia coli | P28630 (AlphaFold model) |
| DNA polymerase III, delta' subunit | E | protein | 334 | Escherichia coli | P28631 (AlphaFold model) |
>1JR3_1 DNA polymerase III subunit gamma (chains A, B, C) MSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARLLAK GLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPARGRF KVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKALDV EQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVSTQAVSAM LGTLDDDQALSLVEAMVEANGERVMALINEAAARGIEWEALLVEMLGLLHRIAMVQLSPA ALGNDMAAIELRMRELARTIPPTDIQLYYQTLLIGRKELPYAPDRRMGVEMTLLRALAFH PRMPLPEPEVPRQ
>1JR3_2 DNA polymerase III, delta subunit (chains D) MIRLYPEQLRAQLNEGLRAAYLLLGNDPLLLQESQDAVRQVAAAQGFEEHHTFSIDPNTD WNAIFSLCQAMSLFASRQTLLLLLPENGPNAAINEQLLTLTGLLHDDLLLIVRGNKLSKA QENAAWFTALANRSVQVTCQTPEQAQLPRWVAARAKQLNLELDDAANQVLCYCYEGNLLA LAQALERLSLLWPDGKLTLPRVEQAVNDAAHFTPFHWVDALLMGKSKRALHILQQLRLEG SEPVILLRTLQRELLLLVNLKRQSAHTPLRALFDKHRVWQNRRGMMGEALNRLSQTQLRQ AVQLLTRTELTLKQDYGQSVWAELEGLSLLLCHKPLADVFIDG
>1JR3_3 DNA polymerase III, delta' subunit (chains E) MRWYPWLRPDFEKLVASYQAGRGHHALLIQALPGMGDDALIYALSRYLLCQQPQGHKSCG HCRGCQLMQAGTHPDYYTLAPEKGKNTLGVDAVREVTEKLNEHARLGGAKVVWVTDAALL TDAAANALLKTLEEPPAETWFFLATREPERLLATLRSRCRLHYLAPPPEQYAVTWLSREV TMSQDALLAALRLSAGSPGAALALFQGDNWQARETLCQALAYSVPSGDWYSLLAALNHEQ APARLHWLATLLMDALKRHHGAAQVTNVDVPGLVAELANHLSPSRLQAILGDVCHIREQL MSVTGINRELLITDLLLRIEHYLQPGVVLPVPHL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Water and common crystallization additives (SO4) are not listed.
Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Jeruzalmi, D., O'Donnell, M., Kuriyan, J. Cell (2001) 106:429-441. DOI 10.1016/S0092-8674(01)00463-9 · PubMed
Other PDB entries of the same protein (UniProt P06710 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1JR3 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.