eF-site ID 6ghk-B
PDB Code 6ghk
Chain B

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Title Human PARP1 (ARTD1) - Catalytic domain in complex with inhibitor ME0527
Classification TRANSFERASE
Compound Poly [ADP-ribose] polymerase 1
Source (PARP1_HUMAN)
Sequence B:  MKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGK
LSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLI
PHDFGMKKPPLLNNADSVQAKAEMLDNLLDIEVAYSLLRG
GSSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTH
ATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWH
GSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVS
KSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLP
KGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDT
SLLYNEYIVYDIAQVNLKYLLKLKFNFKTAHHHHH
Description


Functional site

1) chain B
residue 798
type
sequence K
description binding site for residue SO4 A 1102
source : AC2

2) chain B
residue 875
type
sequence Q
description binding site for residue SO4 A 1102
source : AC2

3) chain B
residue 1012
type
sequence A
description binding site for residue SO4 A 1103
source : AC3

4) chain B
residue 1013
type
sequence H
description binding site for residue SO4 A 1103
source : AC3

5) chain B
residue 865
type
sequence R
description binding site for residue SO4 A 1104
source : AC4

6) chain B
residue 906
type
sequence N
description binding site for residue SO4 A 1104
source : AC4

7) chain B
residue 909
type
sequence H
description binding site for residue SO4 A 1104
source : AC4

8) chain B
residue 1014
type
sequence H
description binding site for residue SO4 A 1105
source : AC5

9) chain B
residue 1016
type
sequence H
description binding site for residue SO4 A 1105
source : AC5

10) chain B
residue 710
type
sequence Y
description binding site for residue EZ2 B 1101
source : AC6

11) chain B
residue 766
type
sequence D
description binding site for residue EZ2 B 1101
source : AC6

12) chain B
residue 862
type
sequence H
description binding site for residue EZ2 B 1101
source : AC6

13) chain B
residue 863
type
sequence G
description binding site for residue EZ2 B 1101
source : AC6

14) chain B
residue 878
type
sequence R
description binding site for residue EZ2 B 1101
source : AC6

15) chain B
residue 880
type
sequence A
description binding site for residue EZ2 B 1101
source : AC6

16) chain B
residue 881
type
sequence P
description binding site for residue EZ2 B 1101
source : AC6

17) chain B
residue 889
type
sequence Y
description binding site for residue EZ2 B 1101
source : AC6

18) chain B
residue 894
type
sequence G
description binding site for residue EZ2 B 1101
source : AC6

19) chain B
residue 896
type
sequence Y
description binding site for residue EZ2 B 1101
source : AC6

20) chain B
residue 897
type
sequence F
description binding site for residue EZ2 B 1101
source : AC6

21) chain B
residue 904
type
sequence S
description binding site for residue EZ2 B 1101
source : AC6

22) chain B
residue 907
type
sequence Y
description binding site for residue EZ2 B 1101
source : AC6

23) chain B
residue 988
type
sequence E
description binding site for residue EZ2 B 1101
source : AC6

24) chain B
residue 702
type
sequence S
description binding site for residue SO4 B 1102
source : AC7

25) chain B
residue 703
type
sequence K
description binding site for residue SO4 B 1102
source : AC7

26) chain B
residue 704
type
sequence R
description binding site for residue SO4 B 1102
source : AC7

27) chain B
residue 903
type
sequence K
description binding site for residue SO4 B 1103
source : AC8

28) chain B
residue 984
type
sequence L
description binding site for residue SO4 B 1103
source : AC8

29) chain B
residue 985
type
sequence L
description binding site for residue SO4 B 1103
source : AC8

30) chain B
residue 986
type
sequence Y
description binding site for residue SO4 B 1103
source : AC8

31) 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

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

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

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

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

36) chain B
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

37) chain B
residue 786
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4

38) 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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