eF-site ID 4zzz-AB
PDB Code 4zzz
Chain A, B

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Title Structure of human PARP1 catalytic domain bound to an isoindolinone inhibitor
Classification TRANSFERASE
Compound POLY [ADP-RIBOSE] POLYMERASE 1
Source (PARP1_HUMAN)
Sequence A:  KSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKL
SKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIP
HDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGG
SDKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHAT
THNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGS
RTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKS
ANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKG
KHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSL
LYNEYIVYDIAQVNLKYLLKLKFNFKTSLW
B:  KLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSK
RQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHD
FGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGDP
IDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAY
DLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNF
AGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCH
TSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVK
GLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEY
IVYDIAQVNLKYLLKLKFNFKT
Description (1)  POLY [ADP-RIBOSE] POLYMERASE 1 (E.C.2.4.2.30)


Functional site

1) chain B
residue 903
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 2012
source : AC1

2) chain B
residue 984
type
sequence L
description BINDING SITE FOR RESIDUE SO4 B 2012
source : AC1

3) chain B
residue 985
type
sequence L
description BINDING SITE FOR RESIDUE SO4 B 2012
source : AC1

4) chain B
residue 986
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 B 2012
source : AC1

5) chain A
residue 903
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 2015
source : AC2

6) chain A
residue 984
type
sequence L
description BINDING SITE FOR RESIDUE SO4 A 2015
source : AC2

7) chain A
residue 985
type
sequence L
description BINDING SITE FOR RESIDUE SO4 A 2015
source : AC2

8) chain A
residue 986
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 2015
source : AC2

9) chain A
residue 858
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 2016
source : AC3

10) chain A
residue 929
type
sequence M
description BINDING SITE FOR RESIDUE SO4 A 2016
source : AC3

11) chain A
residue 949
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 2016
source : AC3

12) chain A
residue 766
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 2017
source : AC4

13) chain A
residue 879
type
sequence I
description BINDING SITE FOR RESIDUE GOL A 2017
source : AC4

14) chain A
residue 880
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 2017
source : AC4

15) chain A
residue 889
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 2017
source : AC4

16) chain A
residue 893
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 2017
source : AC4

17) chain A
residue 894
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 2017
source : AC4

18) chain A
residue 896
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 2017
source : AC4

19) chain A
residue 890
type
sequence M
description BINDING SITE FOR RESIDUE GOL A 2018
source : AC5

20) chain A
residue 896
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 2018
source : AC5

21) chain A
residue 903
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 2018
source : AC5

22) chain A
residue 984
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 2018
source : AC5

23) chain A
residue 988
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 2018
source : AC5

24) chain B
residue 890
type
sequence M
description BINDING SITE FOR RESIDUE GOL B 2013
source : AC6

25) chain B
residue 896
type
sequence Y
description BINDING SITE FOR RESIDUE GOL B 2013
source : AC6

26) chain B
residue 903
type
sequence K
description BINDING SITE FOR RESIDUE GOL B 2013
source : AC6

27) chain B
residue 907
type
sequence Y
description BINDING SITE FOR RESIDUE GOL B 2013
source : AC6

28) chain B
residue 984
type
sequence L
description BINDING SITE FOR RESIDUE GOL B 2013
source : AC6

29) chain B
residue 988
type
sequence E
description BINDING SITE FOR RESIDUE GOL B 2013
source : AC6

30) chain B
residue 858
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 2014
source : AC7

31) chain B
residue 929
type
sequence M
description BINDING SITE FOR RESIDUE SO4 B 2014
source : AC7

32) chain B
residue 949
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 2014
source : AC7

33) chain A
residue 862
type
sequence H
description BINDING SITE FOR RESIDUE FSU A 2019
source : AC8

34) chain A
residue 863
type
sequence G
description BINDING SITE FOR RESIDUE FSU A 2019
source : AC8

35) chain A
residue 896
type
sequence Y
description BINDING SITE FOR RESIDUE FSU A 2019
source : AC8

36) chain A
residue 897
type
sequence F
description BINDING SITE FOR RESIDUE FSU A 2019
source : AC8

37) chain A
residue 904
type
sequence S
description BINDING SITE FOR RESIDUE FSU A 2019
source : AC8

38) chain A
residue 907
type
sequence Y
description BINDING SITE FOR RESIDUE FSU A 2019
source : AC8

39) chain B
residue 862
type
sequence H
description BINDING SITE FOR RESIDUE FSU B 2015
source : AC9

40) chain B
residue 863
type
sequence G
description BINDING SITE FOR RESIDUE FSU B 2015
source : AC9

41) chain B
residue 896
type
sequence Y
description BINDING SITE FOR RESIDUE FSU B 2015
source : AC9

42) chain B
residue 897
type
sequence F
description BINDING SITE FOR RESIDUE FSU B 2015
source : AC9

43) chain B
residue 904
type
sequence S
description BINDING SITE FOR RESIDUE FSU B 2015
source : AC9

44) chain B
residue 907
type
sequence Y
description BINDING SITE FOR RESIDUE FSU B 2015
source : AC9

45) chain B
residue 988
type
sequence E
description BINDING SITE FOR RESIDUE FSU B 2015
source : AC9

46) chain A
residue 988
type ACT_SITE
sequence E
description For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851
source Swiss-Prot : SWS_FT_FI1

47) chain B
residue 988
type ACT_SITE
sequence E
description For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851
source Swiss-Prot : SWS_FT_FI1

48) chain A
residue 862
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:Q9UGN5
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 871
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:Q9UGN5
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 878
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:Q9UGN5
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 904
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:Q9UGN5
source Swiss-Prot : SWS_FT_FI2

52) chain B
residue 862
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:Q9UGN5
source Swiss-Prot : SWS_FT_FI2

53) chain B
residue 871
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:Q9UGN5
source Swiss-Prot : SWS_FT_FI2

54) chain B
residue 878
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:Q9UGN5
source Swiss-Prot : SWS_FT_FI2

55) chain B
residue 904
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:Q9UGN5
source Swiss-Prot : SWS_FT_FI2

56) chain A
residue 782
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

57) chain A
residue 748
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI5

58) chain B
residue 748
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI5


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