1RRJ: DNA topoisomerase I

Structural Mechanisms of Camptothecin Resistance by Mutations in Human Topoisomerase I. Determined by X-ray diffraction at 2.3 Å resolution. Released 6 Jul 2004.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
3
Atoms
6,092
Mol. weight
81.32 kDa
Ligands
TTG, TTC
Released
6 Jul 2004

Explore 1RRJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1RRJ contains 34 α-helices and 23 β-strands across 1 chain. 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: 34 helices, 23 β-strands

ElementResiduesLengthSheet
α-helix205-2073
α-helix209-2124
β-strand220-22121
α-helix2251
β-strand22612
α-helix227-2315
β-strand241-24223
β-strand245-24623
α-helix248-2503
α-helix251-26111
α-helix267-2704
α-helix272-28514
α-helix288-2914
β-strand300-30123
α-helix303-31614
α-helix321-33818
β-strand340-34341
β-strand346-34941
β-strand35014
β-strand35412
α-helix355-3584
β-strand359-36025
β-strand373-37425
α-helix375-3784
α-helix379-3813
β-strand383-38536
α-helix392-3954
β-strand403-40536
β-strand414-41746
α-helix4231
β-strand424-42746
β-strand42914
α-helix434-45118
α-helix454-46310
α-helix464-4663
α-helix470-48415
β-strand50817
α-helix509-5113
β-strand512-51878
β-strand521-530108
α-helix532-5343
β-strand536-54278
α-helix545-55410
β-strand56317
α-helix570-58011
α-helix587-60519
α-helix612-62918
β-strand63319
α-helix640-6423
α-helix643-67028
α-helix681-71030
β-strand71419
α-helix717-7215
α-helix726-73611
α-helix740-7423
α-helix746-7516
α-helix753-7575

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
5'-d(*ap*ap*ap*ap*ap*gp*ap*cp*tp*t*gp*gp*ap*ap*ap*ap*ap*tp*tp*tp*tp*t)-3'BDNA22
5'-d(*ap*ap*ap*ap*ap*tp*tp*tp*tp*tp*cp*cp*ap*ap*gp*tp*cp*tp*tp*tp*tp*t)-3'CDNA22
DNA topoisomerase IAprotein565Homo sapiensP11387 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>1RRJ_1 5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*T*GP*GP*AP*AP*AP*AP*AP*TP*TP*TP*TP*T)-3' (chains B)
AAAAAGACTTGGAAAAATTTTT
Sequence of entity 2 (C), FASTA
>1RRJ_2 5'-D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*CP*AP*AP*GP*TP*CP*TP*TP*TP*TP*T)-3' (chains C)
AAAAATTTTTCCAAGTCTTTTT
Sequence of entity 3 (A), FASTA
>1RRJ_3 DNA topoisomerase I (chains A)
QKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFF
AKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMS
KEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPE
DIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKD
WQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETAD
TVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQP
EDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYN
RANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKT
KKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLSYLDPRITVAWCKKWGVPI
EKIYNKTQREKFAWAIDMADEDYEF

Ligands and cofactors

IDNameFormulaCopies
TTG2-(1-dimethylaminomethyl-2-hydroxy-8-hydroxymethyl-9-oxo-9,11-dihydro-indolizin…C23 H25 N3 O61
TTC(s)-10-[(dimethylamino)methyl]-4-ethyl-4,9-dihydroxy-1H-PYRANO[3',4':6,7]INOLIZ…C23 H23 N3 O51

Primary citation

Mechanisms of camptothecin resistance by human topoisomerase I mutations. Chrencik, J.E., Staker, B.L., Burgin, A.B. et al. J Mol Biol (2004) 339:773-784. DOI 10.1016/j.jmb.2004.03.077 · PubMed

Other PDB entries of the same protein (UniProt P11387 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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