The Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution with rrnA Sequence for the 23S rRNA and Genome-derived Sequences for r-Proteins. Determined by X-ray diffraction at 2.4 Å resolution. Released 20 May 2008.
Explore 3CC2 in 3D Show helices and sheets RCSB PDB PDBe
3CC2 contains 196 α-helices and 194 β-strands across 29 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 | 5-8 | 4 | |
| β-strand | 16-18 | 3 | 7 |
| β-strand | 25-28 | 4 | 7 |
| β-strand | 33-34 | 2 | 7 |
| α-helix | 45-46 | 2 | |
| α-helix | 49-51 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-17 | 13 | |
| α-helix | 20-22 | 3 | |
| α-helix | 23-28 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 15 |
| β-strand | 6-11 | 6 | 16 |
| β-strand | 16-24 | 9 | 16 |
| α-helix | 26-30 | 5 | |
| α-helix | 35-43 | 9 | |
| α-helix | 50-53 | 4 | |
| α-helix | 63 | 1 | |
| β-strand | 64 | 1 | 17 |
| α-helix | 65 | 1 | |
| β-strand | 67-71 | 5 | 16 |
| β-strand | 77-78 | 2 | 16 |
| β-strand | 84 | 1 | 17 |
| β-strand | 89-91 | 3 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-10 | 6 | |
| α-helix | 14-16 | 3 | |
| α-helix | 20-22 | 3 | |
| α-helix | 29-31 | 3 | |
| β-strand | 39-48 | 10 | 1 |
| β-strand | 53-60 | 8 | 1 |
| β-strand | 65-68 | 4 | 1 |
| α-helix | 70 | 1 | |
| β-strand | 71 | 1 | 2 |
| β-strand | 75 | 1 | 3 |
| β-strand | 79-81 | 3 | 1 |
| β-strand | 82 | 1 | 4 |
| β-strand | 93-95 | 3 | 4 |
| α-helix | 96-98 | 3 | |
| α-helix | 100 | 1 | |
| β-strand | 104-106 | 3 | 4 |
| β-strand | 108 | 1 | 5 |
| β-strand | 118 | 1 | 5 |
| β-strand | 126-130 | 5 | 4 |
| β-strand | 136-139 | 4 | 4 |
| β-strand | 145-148 | 4 | 4 |
| β-strand | 153-156 | 4 | 4 |
| α-helix | 158 | 1 | |
| β-strand | 159 | 1 | 2 |
| α-helix | 164-166 | 3 | |
| α-helix | 172-179 | 8 | |
| α-helix | 191-193 | 3 | |
| α-helix | 196-198 | 3 | |
| β-strand | 214-215 | 2 | 6 |
| α-helix | 219-220 | 2 | |
| β-strand | 227-228 | 2 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 37-38 | 2 | 8 |
| β-strand | 41-54 | 14 | 9 |
| β-strand | 66-75 | 10 | 9 |
| β-strand | 79-90 | 12 | 8 |
| β-strand | 93-101 | 9 | 8 |
| α-helix | 109-111 | 3 | |
| α-helix | 121-134 | 14 | |
| β-strand | 137-145 | 9 | 8 |
| α-helix | 148-150 | 3 | |
| β-strand | 161-167 | 7 | 8 |
| α-helix | 171-184 | 14 | |
| β-strand | 187-188 | 2 | 8 |
| α-helix | 190-193 | 4 | |
| β-strand | 199-205 | 7 | 9 |
| α-helix | 206-208 | 3 | |
| β-strand | 211-212 | 2 | 10 |
| α-helix | 214-218 | 5 | |
| α-helix | 220-223 | 4 | |
| α-helix | 225-229 | 5 | |
| β-strand | 255-256 | 2 | 10 |
| β-strand | 261-275 | 15 | 9 |
| α-helix | 279-280 | 2 | |
| β-strand | 284 | 1 | 11 |
| β-strand | 288 | 1 | 11 |
| β-strand | 292-298 | 7 | 9 |
| β-strand | 308-313 | 6 | 9 |
| β-strand | 327-330 | 4 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 12 |
| β-strand | 12-17 | 6 | 12 |
| α-helix | 18-19 | 2 | |
| α-helix | 20-23 | 4 | |
| α-helix | 25-26 | 2 | |
| α-helix | 28-41 | 14 | |
| α-helix | 43-45 | 3 | |
| β-strand | 59 | 1 | 13 |
| β-strand | 72-73 | 2 | 13 |
| β-strand | 76-77 | 2 | 13 |
| α-helix | 86-88 | 3 | |
| α-helix | 104-117 | 14 | |
| α-helix | 121-127 | 7 | |
| β-strand | 138-140 | 3 | 12 |
| α-helix | 142-146 | 5 | |
| α-helix | 150-159 | 10 | |
| α-helix | 164-169 | 6 | |
| β-strand | 173-174 | 2 | 14 |
| α-helix | 178-182 | 5 | |
| β-strand | 186-187 | 2 | 14 |
| β-strand | 193-196 | 4 | 12 |
| α-helix | 202-205 | 4 | |
| β-strand | 211-214 | 4 | 12 |
| α-helix | 220-223 | 4 | |
| α-helix | 225-227 | 3 | |
| β-strand | 233-236 | 4 | 12 |
| α-helix | 237-243 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17-26 | 10 | 18 |
| α-helix | 38-45 | 8 | |
| β-strand | 50-52 | 3 | 18 |
| β-strand | 58 | 1 | 19 |
| β-strand | 62 | 1 | 19 |
| β-strand | 70-75 | 6 | 18 |
| α-helix | 78-87 | 10 | |
| α-helix | 88-90 | 3 | |
| β-strand | 98 | 1 | 18 |
| β-strand | 104-106 | 3 | 18 |
| β-strand | 129-135 | 7 | 18 |
| α-helix | 140-143 | 4 | |
| α-helix | 150-152 | 3 | |
| α-helix | 153-155 | 3 | |
| α-helix | 159-167 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 20 |
| β-strand | 12-16 | 5 | 21 |
| β-strand | 19-24 | 6 | 21 |
| β-strand | 27-32 | 6 | 21 |
| β-strand | 38-43 | 6 | 20 |
| β-strand | 46-51 | 6 | 20 |
| α-helix | 56-76 | 21 | |
| β-strand | 80-87 | 8 | 22 |
| β-strand | 94-97 | 4 | 23 |
| β-strand | 101-105 | 5 | 23 |
| α-helix | 107-109 | 3 | |
| α-helix | 113 | 1 | |
| β-strand | 114-117 | 4 | 23 |
| α-helix | 118-119 | 2 | |
| β-strand | 123-127 | 5 | 22 |
| β-strand | 130-135 | 6 | 22 |
| α-helix | 138-151 | 14 | |
| β-strand | 165-170 | 6 | 22 |
21 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 50S ribosomal protein L2P | A | protein | 240 | Haloarcula marismortui | P20276 (AlphaFold model) |
| 50S ribosomal protein L3P | B | protein | 338 | Haloarcula marismortui | P20279 (AlphaFold model) |
| 50S ribosomal protein L4P | C | protein | 246 | Haloarcula marismortui | P12735 (AlphaFold model) |
| 50S ribosomal protein L5P | D | protein | 177 | Haloarcula marismortui | P14124 (AlphaFold model) |
| 50S ribosomal protein L6P | E | protein | 178 | Haloarcula marismortui | P14135 |
| 50S ribosomal protein L7Ae | F | protein | 120 | Haloarcula marismortui | P12743 |
| 50S ribosomal protein L10E | G | protein | 348 | Haloarcula marismortui | P15825 |
| 50S ribosomal protein L10e | H | protein | 177 | Haloarcula marismortui | P60617 |
| 50S ribosomal protein L11P | I | protein | 162 | Haloarcula marismortui | P14122 |
| 50S ribosomal protein L13P | J | protein | 145 | Haloarcula marismortui | P29198 |
| 50S ribosomal protein L14P | K | protein | 132 | Haloarcula marismortui | P22450 |
| 50S ribosomal protein L15P | L | protein | 165 | Haloarcula marismortui | P12737 |
19 more molecules are not listed.
>3CC2_1 50S ribosomal protein L2P (chains A) MGRRIQGQRRGRGTSTFRAPSHRYKADLEHRKVEDGDVIAGTVVDIEHDPARSAPVAAVE FEDGDRRLILAPEGVGVGDELQVGVSAEIAPGNTLPLAEIPEGVPVCNVESSPGDGGKFA RASGVNAQLLTHDRNVAVVKLPSGEMKRLDPQCRATIGVVAGGGRTDKPFVKAGNKHHKM KARGTKWPNVRGVAMNAVDHPFGGGGRQHPGKPKSISRNAPPGRKVGDIASKRTGRGGNE
>3CC2_2 50S ribosomal protein L3P (chains B) MPQPSRPRKGSLGFGPRKRSTSETPRFNSWPSDDGQPGVQGFAGYKAGMTHVVLVNDEPN SPREGMEETVPVTVIETPPMRAVALRAYEDTPYGQRPLTEVWTDEFHSELDRTLDVPEDH DPDAAEEQIRDAHEAGDLGDLRLITHTVPDAVPSVPKKKPDVMETRVGGGSVSDRLDHAL DIVEDGGEHAMNDIFRAGEYADVAGVTKGKGTQGPVKRWGVQKRKGKHARQGWRRRIGNL GPWNPSRVRSTVPQQGQTGYHQRTELNKRLIDIGEGDEPTVDGGFVNYGEVDGPYTLVKG SVPGPDKRLVRFRPAVRPNDQPRLDPEVRYVSNESNQG
>3CC2_3 50S ribosomal protein L4P (chains C) MQATIYDLDGNTDGEVDLPDVFETPVRSDLIGKAVRAAQANRKQDYGSDEYAGLRTPAES FGSGRGQAHVPKQDGRARRVPQAVKGRSAHPPKTEKDRSLDLNDKERQLAVRSALAATAD ADLVADRGHEFDRDEVPVVVSDDFEDLVKTQEVVSLLEALDVHADIDRADETKIKAGQGS ARGRKYRRPASILFVTSDEPSTAARNLAGADVATASEVNTEDLAPGGAPGRLTVFTESAL AEVAER
>3CC2_4 50S ribosomal protein L5P (chains D) MSSESESGGDFHEMREPRIEKVVVHMGIGHGGRDLANAEDILGEITGQMPVRTKAKRTVG EFDIREGDPIGAKVTLRDEMAEEFLQTALPLAELATSQFDDTGNFSFGVEEHTEFPSQEY DPSIGIYGLDVTVNLVRPGYRVAKRDKASRSIPTKHRLNPADAVAFIESTYDVEVSE
>3CC2_5 50S ribosomal protein L6P (chains E) MPRVELEIPEDVDAEQDHLDITVEGDNGSVTRRLWYPDIDVSVDGDTVVIESDEDNAKTM STIGTFQSHIENMFHGVTEGWEYGMEVFYSHFPMQVNVEGDEVVIENFLGEKAPRRTTIH GDTDVEIDGEELTVSGPDIEAVGQTAADIEQLTRINDKDVRVFQDGVYITRKPNRGDA
>3CC2_6 50S ribosomal protein L7Ae (chains F) MPVYVDFDVPADLEDDALEALEVARDTGAVKKGTNETTKSIERGSAELVFVAEDVQPEEI VMHIPELADEKGVPFIFVEQQDDLGHAAGLEVGSAAAAVTDAGEADADVEDIADKVEELR
>3CC2_7 50S ribosomal protein L10E (chains G) MSAESERKTETIPEWKQEEVDAIVEMIESYESVGVVNIAGIPSRQLQDMRRDLHGTAELR VSRNTLLERALDDVDDGLEDLNGYITGQVGLIGTDDNPFSLFQELEASKTPAPIGAGEVA PNDIVIPEGDTGVDPGPFVGELQSVGADARIQEGSIQVLSDSTVLDTGEEVSQELSNVLN ELGIEPKEVGLDLRAVFADGVLFEPEELELDIDEYRSDIQAAAGRAFNLSVNADYPTATT APTMLQSARGNAKSLALQAAIEDPEVVPDLVSKADAQVRALASQIDDEEALPEELQGVEA DVATEEPTDDQDDDTASEDDADADDAAEEADDDDDDDEDAGDALGAMF
>3CC2_8 50S ribosomal protein L10e (chains H) MSDKPASMYRDIDKPAYTRREYITGIPGSKIAQHKMGRKQKDADDYPVQISLIVEETVQL RHGSLEASRLSANRHLIKELGEEGDYKMTLRKFPHQVLRENKQATGAGADRVSDGMRAAF GKIVGTAARVQAGEQLFTAYCNVEDAEHVKEAFRRAYNKITPSCRIKVERGEELLIA
>3CC2_9 50S ribosomal protein L11P (chains I) MAGTIEVLVPGGEANPGPPLGPELGPTPVDVQAVVQEINDQTAAFDGTEVPVTVKYDDDG SFEIEVGVPPTAELIKDEAGFETGSGEPQEDFVADLSVDQVKQIAEQKHPDLLSYDLTNA AKEVVGTCTSLGVTIEGENPREFKERIDAGEYDDVFAAEAQA
>3CC2_10 50S ribosomal protein L13P (chains J) MSVAEFDADVIVDARDCIMGRVASQVAEQALDGETVAVVNAERAVITGREEQIVEKYEKR VDIGNDNGYFYPKRPDGIFKRTIRGMLPHKKQRGREAFESVRVYLGNPYDEDGEVLDGTS LDRLSNIKFVTLGEISETLGANKTW
>3CC2_11 50S ribosomal protein L14P (chains K) MEALGADVTQGLEKGSLITCADNTGARELKVISVHGYSGTKNRHPKAGLGDKITVSVTKG TPEMRRQVLEAVVVRQRKPIRRPDGTRVKFEDNAAVIVDENEDPRGTELKGPIAREVAQR FGSVASAATMIV
>3CC2_12 50S ribosomal protein L15P (chains L) MTSKKKRQRGSRTHGGGSHKNRRGAGHRGGRGDAGRDKHEFHNHEPLGKSGFKRPQKVQE EAATIDVREIDENVTLLAADDVAEVEDGGFRVDVRDVVEEADDADYVKVLGAGQVRHELT LIADDFSEGAREKVEGAGGSVELTDLGEERQAEAEETEDADADEE
Water and common crystallization additives (K, CL, NA) are not listed.
Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. Blaha, G., Gurel, G., Schroeder, S.J. et al. J Mol Biol (2008) 379:505-519. DOI 10.1016/j.jmb.2008.03.075 · PubMed
Other PDB entries of the same protein (UniProt P20276 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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