eF-site ID 1rr8-C
PDB Code 1rr8
Chain C

click to enlarge
Title Structural Mechanisms of Camptothecin Resistance by Mutations in Human Topoisomerase I
Classification ISOMERASE/DNA
Compound 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'
Source Homo sapiens (Human) (1RR8)
Sequence C:  AAWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKF
YYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFK
DWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMS
KEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGL
SRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHK
WKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKD
WQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALY
FIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDG
QEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQP
EDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQ
QLKELTAPDENIPAKILSYNRANRAVAILCNHQQAPREEN
KQIALGTSKLNXLDPRITVAWCKKWGVPIEKIYNKTQREK
FAWAIDMADEDYEF
Description


Functional site

1) chain C
residue 356
type
sequence E
description BINDING SITE FOR RESIDUE TTG A 1991
source : AC1

2) chain C
residue 364
type
sequence R
description BINDING SITE FOR RESIDUE TTG A 1991
source : AC1

3) chain C
residue 532
type
sequence K
description BINDING SITE FOR RESIDUE TTG A 1991
source : AC1

4) chain C
residue 533
type
sequence D
description BINDING SITE FOR RESIDUE TTG A 1991
source : AC1

5) chain C
residue 718
type
sequence T
description BINDING SITE FOR RESIDUE TTG A 1991
source : AC1

6) chain C
residue 722
type
sequence N
description BINDING SITE FOR RESIDUE TTG A 1991
source : AC1

7) chain C
residue 356
type
sequence E
description BINDING SITE FOR RESIDUE TTC A 100
source : AC2

8) chain C
residue 364
type
sequence R
description BINDING SITE FOR RESIDUE TTC A 100
source : AC2

9) chain C
residue 532
type
sequence K
description BINDING SITE FOR RESIDUE TTC A 100
source : AC2

10) chain C
residue 533
type
sequence D
description BINDING SITE FOR RESIDUE TTC A 100
source : AC2

11) chain C
residue 718
type
sequence T
description BINDING SITE FOR RESIDUE TTC A 100
source : AC2

12) chain C
residue 723
type
sequence X
description BINDING SITE FOR RESIDUE TTC A 100
source : AC2

13) chain C
residue 710-728
type prosite
sequence ENKQIALGTSKLNXLDPRI
description TOPO_IB_1 Topoisomerase (Topo) IB-type active site signature. EnkqialGTSKlnYLdprI
source prosite : PS00176

14) chain C
residue 723
type ACT_SITE
sequence X
description O-(3'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01382, ECO:0000255|PROSITE-ProRule:PRU10130, ECO:0000269|PubMed:10841763, ECO:0000269|PubMed:12426403, ECO:0000269|PubMed:12533542, ECO:0000269|PubMed:15165849, ECO:0000269|PubMed:15801827, ECO:0000269|PubMed:16033260, ECO:0000269|PubMed:9488644
source Swiss-Prot : SWS_FT_FI1

15) chain C
residue 316
type SITE
sequence R
description Interaction with DNA
source Swiss-Prot : SWS_FT_FI2

16) chain C
residue 364
type SITE
sequence R
description Interaction with DNA
source Swiss-Prot : SWS_FT_FI2

17) chain C
residue 412
type SITE
sequence W
description Interaction with DNA
source Swiss-Prot : SWS_FT_FI2

18) chain C
residue 443
type SITE
sequence K
description Interaction with DNA
source Swiss-Prot : SWS_FT_FI2

19) chain C
residue 501
type SITE
sequence T
description Interaction with DNA
source Swiss-Prot : SWS_FT_FI2

20) chain C
residue 532
type SITE
sequence K
description Interaction with DNA
source Swiss-Prot : SWS_FT_FI2

21) chain C
residue 574
type SITE
sequence N
description Interaction with DNA
source Swiss-Prot : SWS_FT_FI2

22) chain C
residue 632
type SITE
sequence H
description Interaction with DNA
source Swiss-Prot : SWS_FT_FI2

23) chain C
residue 280
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

24) chain C
residue 506
type MOD_RES
sequence S
description Phosphoserine; by CK2 => ECO:0000269|PubMed:23185622
source Swiss-Prot : SWS_FT_FI4

25) chain C
residue 204
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI5

26) chain C
residue 549
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI5

27) chain C
residue 712
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI5

28) chain C
residue 336
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI6


Display surface

Download
Links