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1RRJ

Structural Mechanisms of Camptothecin Resistance by Mutations in Human Topoisomerase I

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1B5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*T*GP*GP*AP*AP*AP*AP*AP*TP*TP*TP*TP*T)-3'polymer226806.51
2C5'-D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*CP*AP*AP*GP*TP*CP*TP*TP*TP*TP*T)-3'polymer226690.41
3ADNA topoisomerase Ipolymer56566964.11UniProt (P11387)
Pfam (PF02919)
Pfam (PF01028)
Pfam (PF14370)
In PDB
Homo sapiens (human)
4B2-(1-DIMETHYLAMINOMETHYL-2-HYDROXY-8-HYDROXYMETHYL-9-OXO-9,11-DIHYDRO-INDOLIZINO[1,2-B]QUINOLIN-7-YL)-2-HYDROXY-BUTYRIC ACIDnon-polymer439.51Chemie (TTG)
5B(S)-10-[(DIMETHYLAMINO)METHYL]-4-ETHYL-4,9-DIHYDROXY-1H-PYRANO[3',4':6,7]INOLIZINO[1,2-B]-QUINOLINE-3,14(4H,12H)-DIONEnon-polymer421.41Chemie (TTC)
6waterwater18.0436Chemie (HOH)
Sequence modifications
A: 201 - 765 (UniProt: P11387)
PDBExternal DatabaseDetails
Ser 722Asn 722engineered mutation
Ptr 723Tyr 723modified residue
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains3
Total formula weight80461.0
Non-Polymers*Number of molecules2
Total formula weight860.9
All*Total formula weight81321.9
*Water molecules are not included.

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