eF-site ID 2n8a_58-A
PDB Code 2n8a
Model 58
Chain A

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Title 1H, 13C and 15N chemical shift assignments and solution structure for PARP-1 F1F2 domains in complex with a DNA single-strand break
Classification TRANSFERASE
Compound Poly [ADP-ribose] polymerase 1
Source Homo sapiens (Human) (2N8A)
Sequence A:  MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQ
SPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWD
DQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKS
NRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHP
GCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLP
GVKSEGKRKGDEVD
Description (1)  Poly [ADP-ribose] polymerase 1 (E.C.2.4.2.30)


Functional site

1) chain A
residue 21
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1000
source : AC1

2) chain A
residue 24
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1000
source : AC1

3) chain A
residue 53
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1000
source : AC1

4) chain A
residue 56
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1000
source : AC1

5) chain A
residue 125
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC2

6) chain A
residue 128
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC2

7) chain A
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC2

8) chain A
residue 162
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC2

9) chain A
residue 179
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI10

10) chain A
residue 192
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_FI11

11) chain A
residue 203
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI12

12) chain A
residue 9-93
type ZN_FING
sequence YRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKV
PHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKT
AEAGG
description PARP-type 1 => ECO:0000255|PROSITE-ProRule:PRU00264
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 214
type SITE
sequence D
description Cleavage; by caspase-3 and caspase-7 => ECO:0000269|PubMed:10497198, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:7596430
source Swiss-Prot : SWS_FT_FI5

14) chain A
residue 2
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|Ref.12, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI6

15) chain A
residue 97
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI8

16) chain A
residue 105
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI8

17) chain A
residue 131
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI8

18) chain A
residue 177
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI9

19) chain A
residue 185
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI9

20) chain A
residue 125
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
source Swiss-Prot : SWS_FT_FI4

21) chain A
residue 128
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
source Swiss-Prot : SWS_FT_FI4

22) chain A
residue 159
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
source Swiss-Prot : SWS_FT_FI4

23) chain A
residue 162
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
source Swiss-Prot : SWS_FT_FI4

24) chain A
residue 21-56
type prosite
sequence CKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSC
description ZF_PARP_1 Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature. CKkCsesIpKdslRmaimvqspmfdgkvph..WYHfsC
source prosite : PS00347

25) chain A
residue 125-162
type prosite
sequence CKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGC
description ZF_PARP_1 Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature. CKkCsesIpKdslRmaimvqspmfdgkvph..WYHfsC
source prosite : PS00347

26) chain A
residue 21
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3OD8, ECO:0007744|PDB:3ODA, ECO:0007744|PDB:4AV1, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB
source Swiss-Prot : SWS_FT_FI3

27) chain A
residue 24
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3OD8, ECO:0007744|PDB:3ODA, ECO:0007744|PDB:4AV1, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB
source Swiss-Prot : SWS_FT_FI3

28) chain A
residue 53
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3OD8, ECO:0007744|PDB:3ODA, ECO:0007744|PDB:4AV1, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB
source Swiss-Prot : SWS_FT_FI3

29) chain A
residue 56
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3OD8, ECO:0007744|PDB:3ODA, ECO:0007744|PDB:4AV1, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB
source Swiss-Prot : SWS_FT_FI3

30) chain A
residue 113-203
type ZN_FING
sequence FAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLG
MIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDK
EALKKQLPGVK
description PARP-type 2 => ECO:0000255|PROSITE-ProRule:PRU00264
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 41
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI7


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