Crystal Structure of the E. coli clamp loader bound to Psi Peptide. Determined by X-ray diffraction at 3.89 Å resolution. Released 26 May 2009.
Explore 3GLH in 3D Show helices and sheets RCSB PDB PDBe
3GLH contains 297 α-helices and 117 β-strands across 15 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 | 2-4 | 3 | 1 |
| α-helix | 9-15 | 7 | |
| β-strand | 20-25 | 6 | 1 |
| α-helix | 28-45 | 18 | |
| β-strand | 49-54 | 6 | 1 |
| α-helix | 61-73 | 13 | |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 93-101 | 9 | |
| β-strand | 105 | 1 | 1 |
| β-strand | 108-114 | 7 | 1 |
| α-helix | 116-118 | 3 | |
| α-helix | 125-130 | 6 | |
| β-strand | 135-139 | 5 | 1 |
| α-helix | 146-157 | 12 | |
| 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 | 226-233 | 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 | 6-9 | 4 | |
| α-helix | 15-17 | 3 | |
| α-helix | 22-34 | 13 | |
| β-strand | 40-44 | 5 | 3 |
| β-strand | 47 | 1 | 4 |
| β-strand | 49 | 1 | 4 |
| α-helix | 51-63 | 13 | |
| α-helix | 77-84 | 8 | |
| β-strand | 90-94 | 5 | 3 |
| α-helix | 104-109 | 6 | |
| α-helix | 110-112 | 3 | |
| α-helix | 114-115 | 2 | |
| β-strand | 121-126 | 6 | 3 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 3 |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 3 |
| α-helix | 180-194 | 15 | |
| β-strand | 198 | 1 | 5 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-228 | 15 | |
| β-strand | 232 | 1 | 5 |
| 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 |
|---|---|---|---|
| α-helix | 6-9 | 4 | |
| α-helix | 22-34 | 13 | |
| β-strand | 40-44 | 5 | 6 |
| α-helix | 51-62 | 12 | |
| α-helix | 77-83 | 7 | |
| β-strand | 91-94 | 4 | 6 |
| α-helix | 104-110 | 7 | |
| α-helix | 114-115 | 2 | |
| β-strand | 121-126 | 6 | 6 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-144 | 12 | |
| β-strand | 150-156 | 7 | 6 |
| α-helix | 159-161 | 3 | |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 6 |
| α-helix | 180-194 | 15 | |
| β-strand | 198 | 1 | 7 |
| α-helix | 200-209 | 10 | |
| α-helix | 214-227 | 14 | |
| β-strand | 232 | 1 | 7 |
| 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 | 15-17 | 3 | |
| α-helix | 22-34 | 13 | |
| β-strand | 40-44 | 5 | 8 |
| α-helix | 51-63 | 13 | |
| α-helix | 77-84 | 8 | |
| β-strand | 91-94 | 4 | 8 |
| α-helix | 104-107 | 4 | |
| α-helix | 114-115 | 2 | |
| β-strand | 121-126 | 6 | 8 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-143 | 11 | |
| β-strand | 150-155 | 6 | 8 |
| α-helix | 164-167 | 4 | |
| β-strand | 171-174 | 4 | 8 |
| 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 | 234-240 | 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 | 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 | 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 delta | A, F, K | protein | 343 | Escherichia coli | P28630 (AlphaFold model) |
| DNA polymerase III subunit tau | B, C, D, G, H, I, L, M, N | protein | 376 | Escherichia coli | P06710 (AlphaFold model) |
| DNA polymerase III subunit delta' | E, J, O | protein | 334 | Escherichia coli | P28631 (AlphaFold model) |
>3GLH_1 DNA polymerase III subunit delta (chains A, F, K) MIRLYPEQLRAQLNEGLRAAYLLLGNDPLLLQESQDAVRQVAAAQGFEEHHTFSIDPNTD WNAIFSLCQAMSLFASRQTLLLLLPENGPNAAINEQLLTLTGLLHDDLLLIVRGNKLSKA QENAAWFTALANRSVQVTCQTPEQAQLPRWVAARAKQLNLELDDAANQVLCYCYEGNLLA LAQALERLSLLWPDGKLTLPRVEQAVNDAAHFTPFHWVDALLMGKSKRALHILQQLRLEG SEPVILLRTLQRELLLLVNLKRQSAHTPLRALFDKHRVWQNRRGMMGEALNRLSQTQLRQ AVQLLTRTELTLKQDYGQSVWAELEGLSLLLCHKPLADVFIDG
>3GLH_2 DNA polymerase III subunit tau (chains B, C, D, G, H, I, L, M, N) GPHMSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARL LAKGLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPAR GRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKA LDVEQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVSTQAV SAMLGTLDDDQALSLVEAMVEANGERVMALINEAAARGIEWEALLVEMLGLLHRIAMVQL SPAALGNDMAAIELRMRELARTIPPTDIQLYYQTLLIGRKELPYAPDRRMGVEMTLLRAL AFHPRMPLPEPEVPRQ
>3GLH_3 DNA polymerase III subunit delta' (chains E, J, O) MRWYPWLRPDFEKLVASYQAGRGHHALLIQALPGMGDDALIYALSRYLLCQQPQGHKSCG HCRGCQLMQAGTHPDYYTLAPEKGKNTLGVDAVREVTEKLNEHARLGGAKVVWVTDAALL TDAAANALLKTLEEPPAETWFFLATREPERLLATLRSRCRLHYLAPPPEQYAVTWLSREV TMSQDALLAALRLSAGSPGAALALFQGDNWQARETLCQALAYSVPSGDWYSLLAALNHEQ APARLHWLATLLMDALKRHHGAAQVTNVDVPGLVAELANHLSPSRLQAILGDVCHIREQL MSVTGINRELLITDLLLRIEHYLQPGVVLPVPHL
The mechanism of ATP-dependent primer-template recognition by a clamp loader complex. Simonetta, K.R., Kazmirski, S.L., Goedken, E.R. et al. Cell (2009) 137:659-671. DOI 10.1016/j.cell.2009.03.044 · PubMed
Other PDB entries of the same protein (UniProt P28630 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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