2ZJP: Thiopeptide antibiotic Nosiheptide
Thiopeptide antibiotic Nosiheptide bound to the large ribosomal subunit of Deinococcus radiodurans. Determined by X-ray diffraction at 3.7 Å resolution. Released 17 Jun 2008.
- Method
- X-ray diffraction
- Resolution
- 3.7 Å
- Organisms
- DEINOCOCCUS RADIODURANS, STREPTOMYCES ACTUOSUS
- Chains
- 31
- Atoms
- 84,444
- Mol. weight
- 1366.82 kDa
- Ligands
- ZN, MG, NO1
- Released
- 17 Jun 2008
Explore 2ZJP in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2ZJP contains 84 α-helices and 182 β-strands across 25 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 4: 0 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-3 | 2 | 3 |
| β-strand | 15 | 1 | 4 |
| β-strand | 24-25 | 2 | 3 |
| β-strand | 26 | 1 | 4 |
| β-strand | 34-35 | 2 | 3 |
Chain A: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 44 | 1 | 7 |
| β-strand | 49 | 1 | 7 |
| β-strand | 76-85 | 10 | 8 |
| β-strand | 90-97 | 8 | 8 |
| β-strand | 105-106 | 2 | 8 |
| β-strand | 116-118 | 3 | 8 |
| β-strand | 127 | 1 | 9 |
| β-strand | 130 | 1 | 9 |
| β-strand | 142-143 | 2 | 9 |
| β-strand | 163 | 1 | 9 |
| β-strand | 165-168 | 4 | 10 |
| β-strand | 172-176 | 5 | 10 |
| β-strand | 182-186 | 5 | 10 |
| β-strand | 192-193 | 2 | 9 |
| α-helix | 211-214 | 4 | |
| α-helix | 223-225 | 3 | |
| α-helix | 262-265 | 4 | |
| β-strand | 267-268 | 2 | 10 |
Chain B: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-14 | 12 | 11 |
| β-strand | 21-27 | 7 | 11 |
| β-strand | 31-32 | 2 | 12 |
| β-strand | 33-37 | 5 | 13 |
| β-strand | 46-50 | 5 | 13 |
| α-helix | 56-58 | 3 | |
| α-helix | 61-68 | 8 | |
| β-strand | 78-79 | 2 | 13 |
| β-strand | 89-90 | 2 | 12 |
| β-strand | 101-107 | 7 | 11 |
| α-helix | 108-109 | 2 | |
| β-strand | 110-113 | 4 | 14 |
| β-strand | 159-161 | 3 | 14 |
| β-strand | 164-166 | 3 | 11 |
| β-strand | 170-171 | 2 | 11 |
| β-strand | 174-176 | 3 | 11 |
| β-strand | 181-185 | 5 | 11 |
| β-strand | 195-200 | 6 | 11 |
Chain C: 6 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 24-38 | 15 | |
| α-helix | 94-96 | 3 | |
| α-helix | 97-112 | 16 | |
| β-strand | 118 | 1 | 15 |
| α-helix | 131-138 | 8 | |
| β-strand | 149-151 | 3 | 16 |
| α-helix | 155-158 | 4 | |
| β-strand | 169-170 | 2 | 16 |
| α-helix | 177-182 | 6 | |
| β-strand | 186-187 | 2 | 16 |
| β-strand | 189 | 1 | 15 |
Chain D: 10 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-7 | 2 | |
| α-helix | 8-12 | 5 | |
| α-helix | 13-17 | 5 | |
| β-strand | 33-37 | 5 | 17 |
| α-helix | 49-57 | 9 | |
| α-helix | 58-62 | 5 | |
| α-helix | 64-65 | 2 | |
| β-strand | 66 | 1 | 18 |
| β-strand | 69 | 1 | 19 |
| β-strand | 84 | 1 | 19 |
| β-strand | 88 | 1 | 18 |
| β-strand | 90-91 | 2 | 17 |
| α-helix | 94-102 | 9 | |
| α-helix | 103-107 | 5 | |
| β-strand | 117 | 1 | 20 |
| β-strand | 129-130 | 2 | 17 |
| α-helix | 143-145 | 3 | |
| β-strand | 153-157 | 5 | 17 |
| α-helix | 163-173 | 11 | |
| β-strand | 177 | 1 | 20 |
Chain E: 3 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 17-18 | 2 | 21 |
| β-strand | 23-26 | 4 | 21 |
| β-strand | 33-36 | 4 | 21 |
| β-strand | 44 | 1 | 22 |
| β-strand | 51 | 1 | 22 |
| α-helix | 60-81 | 22 | |
| β-strand | 83-90 | 8 | 23 |
| β-strand | 95-96 | 2 | 24 |
| β-strand | 99 | 1 | 25 |
| β-strand | 102 | 1 | 25 |
| β-strand | 104-106 | 3 | 24 |
| β-strand | 113-114 | 2 | 24 |
| β-strand | 121-124 | 4 | 23 |
| β-strand | 130-135 | 6 | 23 |
| α-helix | 138-151 | 14 | |
| α-helix | 153-155 | 3 | |
| β-strand | 161-163 | 3 | 23 |
Chain F: 5 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-10 | 3 | 26 |
| α-helix | 35-44 | 10 | |
| β-strand | 55-57 | 3 | 26 |
| β-strand | 59 | 1 | 27 |
| β-strand | 65 | 1 | 27 |
| β-strand | 68-69 | 2 | 26 |
| α-helix | 75-82 | 8 | |
| β-strand | 97-98 | 2 | 28 |
| α-helix | 101-104 | 4 | |
| α-helix | 121-134 | 14 | |
| β-strand | 136-137 | 2 | 28 |
| α-helix | 138-139 | 2 | |
Chain G: 5 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 41-45 | 5 | 29 |
| α-helix | 51-63 | 13 | |
| β-strand | 79-83 | 5 | 29 |
| β-strand | 99-102 | 4 | 30 |
| β-strand | 112-115 | 4 | 30 |
| α-helix | 116-118 | 3 | |
| α-helix | 123-131 | 9 | |
| α-helix | 139-145 | 7 | |
| β-strand | 148-150 | 3 | 29 |
| α-helix | 157-160 | 4 | |
17 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 |
|---|
| 50S ribosomal protein L33 | 1 | protein | 55 | DEINOCOCCUS RADIODURANS | Q9RSS4 (AlphaFold model) |
| 50S ribosomal protein L34 | 2 | protein | 47 | DEINOCOCCUS RADIODURANS | Q9RSH2 (AlphaFold model) |
| 50S ribosomal protein L35 | 3 | protein | 66 | DEINOCOCCUS RADIODURANS | Q9RSW6 (AlphaFold model) |
| 50S ribosomal protein L36 | 4 | protein | 37 | DEINOCOCCUS RADIODURANS | Q9RSK0 (AlphaFold model) |
| Nosiheptide | 5 | protein | 13 | STREPTOMYCES ACTUOSUS | C6FX52 |
| 50S ribosomal protein L2 | A | protein | 274 | DEINOCOCCUS RADIODURANS | Q9RXJ9 |
| 50S ribosomal protein L3 | B | protein | 211 | DEINOCOCCUS RADIODURANS | Q9RXK2 |
| 50S ribosomal protein L4 | C | protein | 205 | DEINOCOCCUS RADIODURANS | Q9RXK1 |
| 50S ribosomal protein L5 | D | protein | 180 | DEINOCOCCUS RADIODURANS | Q9RXJ0 |
| 50S ribosomal protein L6 | E | protein | 185 | DEINOCOCCUS RADIODURANS | Q9RSL3 |
| 50S ribosomal protein L11 | F | protein | 144 | DEINOCOCCUS RADIODURANS | Q9RSS7 |
| 50S ribosomal protein L13 | G | protein | 174 | DEINOCOCCUS RADIODURANS | Q9RXY1 |
19 more molecules are not listed.
Sequence of entity 1 (1), FASTA
>2ZJP_1 50S RIBOSOMAL PROTEIN L33 (chains 1)
MAKDGPRIIVKMESSAGTGFYYTTTKNRRNTQAKLELKKYDPVAKKHVVFREKKV
Sequence of entity 2 (2), FASTA
>2ZJP_2 50S RIBOSOMAL PROTEIN L34 (chains 2)
MKRTYQPNNRKRAKTHGFRARMKTKSGRNILARRRAKGRHQLTVSDE
Sequence of entity 3 (3), FASTA
>2ZJP_3 50S RIBOSOMAL PROTEIN L35 (chains 3)
MPKMKTHKMAKRRIKITGTGKVMAFKSGKRHQNTGKSGDEIRGKGKGFVLAKAEWARMKL
MLPRGK
Sequence of entity 4 (4), FASTA
>2ZJP_4 50S RIBOSOMAL PROTEIN L36 (chains 4)
MKVRSSVKKMCDNCKVVRRHGRVLVICSNVKHKQRQG
Sequence of entity 5 (5), FASTA
>2ZJP_5 NOSIHEPTIDE (chains 5)
SCTTCECCCSCSX
Sequence of entity 6 (A), FASTA
>2ZJP_6 50S RIBOSOMAL PROTEIN L2 (chains A)
AVKKYRPYTPSRRQMTTADFSGLTKKRPEKALTEALPKTGGRNNRGRITSRFIGGGHKRL
YRIIDFKRRDKSGVNAKVAAIEYDPNRSARIALLHYADGEKRYILAPEGLTVGATVNAGP
EAEPKLGNALPLRFVPVGAVVHALELVPGKGAQLARSAGTSVQVQGKESDYVIVRLPSGE
LRRVHSECYATIGAVGNAEHKNIVLGKAGRSRWLGRKPHQRGSAMNPVDHPHGGGEGRTG
AGRVPVTPWGKPTKGLKTRRKRKTSDRFIVTRRK
Sequence of entity 7 (B), FASTA
>2ZJP_7 50S RIBOSOMAL PROTEIN L3 (chains B)
MKGILGTKIGMTQIWKNDRAIPVTVVLAGPCPIVQRKTAQTDGYEAVQIGYAPKAERKVN
KPMQGHFAKAGVAPTRILREFRGFAPDGDSVNVDIFAEGEKIDATGTSKGKGTQGVMKRW
NFAGGPASHGSKKWHRRPGSIGQRKTPGRVYKGKRMAGHMGMERVTVQNLEVVEIRAGEN
LILVKGAIPGANGGLVVLRSAAKASAAKGGK
Sequence of entity 8 (C), FASTA
>2ZJP_8 50S RIBOSOMAL PROTEIN L4 (chains C)
MAQINVIGQNGGRTIELPLPEVNSGVLHEVVTWQLASRRRGTASTRTRAQVSKTGRKMYG
QKGTGNARHGDRSVPTFVGGGVAFGPKPRSYDYTLPRQVRQLGLAMAIASRQEGGKLVAV
DGFDIADAKTKNFISWAKQNGLDGTEKVLLVTDDENTRRAARNVSWVSVLPVAGVNVYDI
LRHDRLVIDAAALEIVEEEAGEEQQ
Sequence of entity 9 (D), FASTA
>2ZJP_9 50S RIBOSOMAL PROTEIN L5 (chains D)
MQQLKTKYNDQVRPALMQQFGYSSVMAVPRIEKIVVNEGLGSSKEDSKAIDKAAKELALI
TLQKPIITKAKKSISNFKLRQGMPVGIKVTLRGERMYVFLEKLINIGLPRIRDFRGINPN
AFDGRGNYNLGIKEQLIFPEITYDMVDKTRGMDITIVTTAKTDEEARALLQSMGLPFRKQ
Sequence of entity 10 (E), FASTA
>2ZJP_10 50S RIBOSOMAL PROTEIN L6 (chains E)
MSRIGKQPIAVPSGVTVNAQDGVFKVKGPKGELTVPYNTELTVRQDGDQLLVERPSDAQK
HRALHGLTRTLVANAVKGVSDGYTINLELRGVGFRAKLTGKALEMNIGYSHPVIIEPPAG
VTFAVPEPTRIDVSGIDKQLVGQVAANVRKVRKPDAYHGKGVRFVGEQIALKAGKAGATG
GKGKK
Sequence of entity 11 (F), FASTA
>2ZJP_11 50S RIBOSOMAL PROTEIN L11 (chains F)
MKKVAGIVKLQLPAGKATPAPPVGPALGQYGANIMEFTKAFNAQTADKGDAIIPVEITIY
ADRSFTFITKTPPMSYLIRKAAGIGKGSSTPNKAKVGKLNWDQVLEIAKTKMPDLNAGSV
EAAANTVAGTARSMGVTVEGGPNA
Sequence of entity 12 (G), FASTA
>2ZJP_12 50S RIBOSOMAL PROTEIN L13 (chains G)
MAFPDTDVSPPRGGPSSPAKSPLLRSFKVKTYIPKNDEQNWVVVDASGVPLGRLATLIAS
RIRGKHRPDFTPNMIQGDFVVVINAAQVALTGKKLDDKVYTRYTGYQGGLKTETAREALS
KHPERVIEHAVFGMLPKGRQGRAMHTRLKVYAGETHPHSAQKPQVLKTQPLEVK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 2 |
| MG | Magnesium ion | Mg | 35 |
| NO1 | 4-(hydroxymethyl)-3-methyl-1H-indole-2-carboxylic acid | C11 H11 N O3 | 1 |
Primary citation
Translational Regulation Via L11: Molecular Switches on the Ribosome Turned on and Off by Thiostrepton and Micrococcin. Harms, J.M., Wilson, D.N., Schluenzen, F. et al. Mol Cell (2008) 30:26. DOI 10.1016/J.MOLCEL.2008.01.009 · PubMed
Other PDB entries of the same protein (UniProt Q9RSS4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5DM6 2.9 Å, Crystal structure of the 50S ribosomal subunit from Deinococcus radiodurans
- 2ZJR 2.91 Å, Refined native structure of the large ribosomal subunit (50S) from Deinococcus radiodurans
- 5DM7 3.0 Å, Crystal structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex…
- 1NKW 3.1 Å, Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans
- 4IO9 3.2 Å, Crystal structure of compound 4d bound to large ribosomal subunit (50S) from Deinococcus…
- 4IOA 3.2 Å, Crystal structure of compound 4e bound to large ribosomal subunit (50S) from Deinococcus…
- 7A0S 3.22 Å, 50S Deinococcus radiodurans ribosome bounded with mycinamicin I
- 3PIO 3.25 Å, Crystal structure of the synergistic antibiotic pair lankamycin and lankacidin in…
- 1NWY 3.3 Å, Complex of the large ribosomal subunit from deinococcus radiodurans with azithromycin
- 2ZJQ 3.3 Å, Interaction of L7 with L11 induced by Microccocin binding to the Deinococcus radiodurans…
- 3CF5 3.3 Å, Thiopeptide antibiotic Thiostrepton bound to the large ribosomal subunit of Deinococcus…
- 7A0R 3.3 Å, 50S Deinococcus radiodurans ribosome bounded with mycinamicin I
Browse structure collections
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