1XXH: ATPgS Bound E. Coli Clamp Loader Complex
ATPgS Bound E. Coli Clamp Loader Complex. Determined by X-ray diffraction at 3.45 Å resolution. Released 7 Dec 2004.
- Method
- X-ray diffraction
- Resolution
- 3.45 Å
- Organism
- Escherichia coli
- Chains
- 10
- Atoms
- 27,736
- Mol. weight
- 404.36 kDa
- Ligands
- PO4, AGS, ZN
- Released
- 7 Dec 2004
Explore 1XXH in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1XXH contains 198 α-helices and 78 β-strands across 10 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: 18 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 1 |
| α-helix | 6-15 | 10 | |
| β-strand | 20-25 | 6 | 1 |
| α-helix | 28-42 | 15 | |
| β-strand | 51-54 | 4 | 1 |
| α-helix | 61-69 | 9 | |
| α-helix | 70-72 | 3 | |
| β-strand | 79-83 | 5 | 1 |
| α-helix | 93-99 | 7 | |
| β-strand | 109-114 | 6 | 1 |
| α-helix | 121-123 | 3 | |
| α-helix | 126-130 | 5 | |
| β-strand | 135-139 | 5 | 1 |
| α-helix | 147-157 | 11 | |
| β-strand | 161-162 | 2 | 2 |
| α-helix | 164-172 | 9 | |
| α-helix | 178-191 | 14 | |
| β-strand | 196-197 | 2 | 2 |
| α-helix | 199-209 | 11 | |
| α-helix | 214-221 | 8 | |
| α-helix | 226-235 | 10 | |
| α-helix | 243-262 | 20 | |
| α-helix | 269-276 | 8 | |
| α-helix | 285-292 | 8 | |
| α-helix | 295-314 | 20 | |
| α-helix | 321-330 | 10 | |
Chain B: 23 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-9 | 4 | |
| α-helix | 15-17 | 3 | |
| α-helix | 22-33 | 12 | |
| β-strand | 41-44 | 4 | 3 |
| α-helix | 51-62 | 12 | |
| α-helix | 77-84 | 8 | |
| β-strand | 90-94 | 5 | 3 |
| α-helix | 103-109 | 7 | |
| β-strand | 122-126 | 5 | 3 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 152-156 | 5 | 3 |
| α-helix | 164-168 | 5 | |
| β-strand | 171-174 | 4 | 3 |
| α-helix | 175-176 | 2 | |
| α-helix | 180-192 | 13 | |
| β-strand | 198 | 1 | 4 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-228 | 15 | |
| β-strand | 232 | 1 | 4 |
| α-helix | 234-240 | 7 | |
| α-helix | 248-254 | 7 | |
| α-helix | 255-259 | 5 | |
| α-helix | 261-274 | 14 | |
| α-helix | 279-295 | 17 | |
| α-helix | 304-306 | 3 | |
| α-helix | 310-319 | 10 | |
| α-helix | 322-338 | 17 | |
| α-helix | 339-341 | 3 | |
| α-helix | 345-358 | 14 | |
Chain C: 20 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-9 | 4 | |
| α-helix | 23-34 | 12 | |
| β-strand | 40-44 | 5 | 5 |
| β-strand | 47 | 1 | 6 |
| β-strand | 49 | 1 | 6 |
| α-helix | 51-59 | 9 | |
| α-helix | 77-82 | 6 | |
| β-strand | 87 | 1 | 5 |
| β-strand | 90-94 | 5 | 5 |
| α-helix | 101-109 | 9 | |
| β-strand | 121-126 | 6 | 5 |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 5 |
| α-helix | 164-167 | 4 | |
| β-strand | 171 | 1 | 5 |
| β-strand | 174 | 1 | 5 |
| α-helix | 176-179 | 4 | |
| α-helix | 180-192 | 13 | |
| β-strand | 197-198 | 2 | 7 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-227 | 14 | |
| β-strand | 231-232 | 2 | 7 |
| α-helix | 234-241 | 8 | |
| α-helix | 246-257 | 12 | |
| α-helix | 263-273 | 11 | |
| α-helix | 278-295 | 18 | |
| α-helix | 307-319 | 13 | |
| α-helix | 322-338 | 17 | |
| α-helix | 339-341 | 3 | |
| α-helix | 345-358 | 14 | |
| α-helix | 364-366 | 3 | |
Chain D: 22 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-9 | 4 | |
| α-helix | 15-17 | 3 | |
| α-helix | 22-32 | 11 | |
| β-strand | 40-45 | 6 | 8 |
| α-helix | 51-62 | 12 | |
| α-helix | 77-84 | 8 | |
| β-strand | 90-94 | 5 | 8 |
| α-helix | 101-109 | 9 | |
| β-strand | 121-126 | 6 | 8 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 8 |
| α-helix | 159-161 | 3 | |
| α-helix | 164-169 | 6 | |
| β-strand | 171-175 | 5 | 8 |
| α-helix | 176-179 | 4 | |
| α-helix | 180-193 | 14 | |
| β-strand | 197-198 | 2 | 9 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-227 | 14 | |
| β-strand | 231-232 | 2 | 9 |
| α-helix | 234-241 | 8 | |
| α-helix | 248-258 | 11 | |
| α-helix | 262-272 | 11 | |
| α-helix | 279-297 | 19 | |
| α-helix | 305-308 | 4 | |
| α-helix | 310-319 | 10 | |
| α-helix | 322-338 | 17 | |
| α-helix | 345-358 | 14 | |
Chain E: 19 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 26-30 | 5 | 10 |
| α-helix | 37-48 | 12 | |
| α-helix | 63-70 | 8 | |
| β-strand | 76-78 | 3 | 10 |
| β-strand | 88 | 1 | 11 |
| α-helix | 90-101 | 12 | |
| α-helix | 103-104 | 2 | |
| β-strand | 110-113 | 4 | 10 |
| α-helix | 117-119 | 3 | |
| β-strand | 120 | 1 | 11 |
| α-helix | 122-133 | 12 | |
| β-strand | 139-145 | 7 | 10 |
| α-helix | 153-156 | 4 | |
| 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 | 230-232 | 3 | |
| α-helix | 233-236 | 4 | |
| α-helix | 241-259 | 19 | |
| α-helix | 271-280 | 10 | |
| α-helix | 283-302 | 20 | |
| α-helix | 309-323 | 15 | |
Chain F: 17 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 12 |
| α-helix | 9-15 | 7 | |
| β-strand | 20-25 | 6 | 12 |
| α-helix | 28-42 | 15 | |
| β-strand | 51-52 | 2 | 12 |
| α-helix | 61-70 | 10 | |
| β-strand | 79-83 | 5 | 12 |
| α-helix | 93-96 | 4 | |
| α-helix | 98-101 | 4 | |
| β-strand | 109-114 | 6 | 12 |
| α-helix | 125-130 | 6 | |
| β-strand | 135-139 | 5 | 12 |
| α-helix | 147-156 | 10 | |
| β-strand | 161-162 | 2 | 13 |
| α-helix | 164-172 | 9 | |
| α-helix | 178-191 | 14 | |
| β-strand | 196-197 | 2 | 13 |
| α-helix | 199-208 | 10 | |
| α-helix | 216-220 | 5 | |
| α-helix | 226-235 | 10 | |
| α-helix | 243-261 | 19 | |
| α-helix | 269-275 | 7 | |
| α-helix | 282-292 | 11 | |
| α-helix | 295-314 | 20 | |
| α-helix | 320-330 | 11 | |
Chain G: 19 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-9 | 4 | |
| α-helix | 22-32 | 11 | |
| β-strand | 40-44 | 5 | 14 |
| α-helix | 51-62 | 12 | |
| α-helix | 77-84 | 8 | |
| β-strand | 90-94 | 5 | 14 |
| α-helix | 103-107 | 5 | |
| β-strand | 121-126 | 6 | 14 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 14 |
| α-helix | 159-161 | 3 | |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 14 |
| α-helix | 180-190 | 11 | |
| β-strand | 198 | 1 | 15 |
| α-helix | 204-207 | 4 | |
| α-helix | 214-227 | 14 | |
| β-strand | 232 | 1 | 15 |
| α-helix | 234-237 | 4 | |
| α-helix | 248-257 | 10 | |
| α-helix | 261-272 | 12 | |
| α-helix | 278-295 | 18 | |
| α-helix | 310-319 | 10 | |
| α-helix | 322-338 | 17 | |
| α-helix | 345-359 | 15 | |
Chain H: 20 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-9 | 4 | |
| α-helix | 23-34 | 12 | |
| β-strand | 40-44 | 5 | 16 |
| β-strand | 47 | 1 | 17 |
| β-strand | 49 | 1 | 17 |
| α-helix | 51-59 | 9 | |
| α-helix | 77-82 | 6 | |
| β-strand | 91-94 | 4 | 16 |
| α-helix | 101-109 | 9 | |
| β-strand | 121-126 | 6 | 16 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-140 | 8 | |
| β-strand | 150-156 | 7 | 16 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-174 | 2 | 16 |
| α-helix | 176-179 | 4 | |
| α-helix | 180-193 | 14 | |
| β-strand | 198 | 1 | 18 |
| α-helix | 203-209 | 7 | |
| α-helix | 214-227 | 14 | |
| β-strand | 232 | 1 | 18 |
| α-helix | 234-240 | 7 | |
| α-helix | 246-257 | 12 | |
| α-helix | 261-272 | 12 | |
| α-helix | 278-294 | 17 | |
| α-helix | 307-319 | 13 | |
| α-helix | 322-338 | 17 | |
| α-helix | 339-341 | 3 | |
| α-helix | 345-358 | 14 | |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| DNA polymerase III, delta subunit | A, F | protein | 343 | Escherichia coli | P28630 (AlphaFold model) |
| DNA polymerase III subunit gamma | B, C, D, G, H, I | protein | 373 | Escherichia coli | P06710 (AlphaFold model) |
| DNA polymerase III, delta prime subunit | E, J | protein | 334 | Escherichia coli | P28631 (AlphaFold model) |
Sequence of entity 1 (A, F), FASTA
>1XXH_1 DNA polymerase III, delta subunit (chains A, F)
MIRLYPEQLRAQLNEGLRAAYLLLGNDPLLLQESQDAVRQVAAAQGFEEHHTFSIDPNTD
WNAIFSLCQAMSLFASRQTLLLLLPENGPNAAINEQLLTLTGLLHDDLLLIVRGNKLSKA
QENAAWFTALANRSVQVTCQTPEQAQLPRWVAARAKQLNLELDDAANQVLCYCYEGNLLA
LAQALERLSLLWPDGKLTLPRVEQAVNDAAHFTPFHWVDALLMGKSKRALHILQQLRLEG
SEPVILLRTLQRELLLLVNLKRQSAHTPLRALFDKHRVWQNRRGMMGEALNRLSQTQLRQ
AVQLLTRTELTLKQDYGQSVWAELEGLSLLLCHKPLADVFIDG
Sequence of entity 2 (B, C, D, G, H, I), FASTA
>1XXH_2 DNA polymerase III subunit gamma (chains B, C, D, G, H, I)
MSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARLLAK
GLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPARGRF
KVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKALDV
EQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVSTQAVSAM
LGTLDDDQALSLVEAMVEANGERVMALINEAAARGIEWEALLVEMLGLLHRIAMVQLSPA
ALGNDMAAIELRMRELARTIPPTDIQLYYQTLLIGRKELPYAPDRRMGVEMTLLRALAFH
PRMPLPEPEVPRQ
Sequence of entity 3 (E, J), FASTA
>1XXH_3 DNA polymerase III, delta prime subunit (chains E, J)
MRWYPWLRPDFEKLVASYQAGRGHHALLIQALPGMGDDALIYALSRYLLCQQPQGHKSCG
HCRGCQLMQAGTHPDYYTLAPEKGKNTLGVDAVREVTEKLNEHARLGGAKVVWVTDAALL
TDAAANALLKTLEEPPAETWFFLATREPERLLATLRSRCRLHYLAPPPEQYAVTWLSREV
TMSQDALLAALRLSAGSPGAALALFQGDNWQARETLCQALAYSVPSGDWYSLLAALNHEQ
APARLHWLATLLMDALKRHHGAAQVTNVDVPGLVAELANHLSPSRLQAILGDVCHIREQL
MSVTGINRELLITDLLLRIEHYLQPGVVLPVPHL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PO4 | Phosphate ion | O4 P | 2 |
| AGS | Phosphothiophosphoric acid-adenylate ester | C10 H16 N5 O12 P3 S | 4 |
| ZN | Zinc ion | Zn | 8 |
Primary citation
Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex. Kazmirski, S.L., Podobnik, M., Weitze, T.F. et al. Proc Natl Acad Sci U S A (2004) 101:16750-16755. DOI 10.1073/pnas.0407904101 · PubMed
Other PDB entries of the same protein (UniProt P28630 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1JQL 2.5 Å, Mechanism of Processivity Clamp Opening by the Delta Subunit Wrench of the Clamp Loader…
- 9OYJ 2.53 Å, Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped…
- 9OYH 2.54 Å, Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped…
- 9OYI 2.54 Å, Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped…
- 8GJ2 2.6 Å, E. coli clamp loader with closed clamp on primed template DNA
- 9OYK 2.6 Å, Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped…
- 9OYM 2.6 Å, Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped…
- 1JR3 2.7 Å, Crystal Structure of the Processivity Clamp Loader Gamma Complex of E. coli DNA…
- 8GIZ 2.7 Å, E. coli clamp loader with open clamp
- 9OYN 2.7 Å, Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped…
- 9OYC 2.71 Å, Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 1-nt gapped…
- 9OYE 2.72 Å, Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 1-nt gapped…
Browse structure collections
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