eF-site ID 2l31_12-A
PDB Code 2l31
Model 12
Chain A

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Title Human PARP-1 zinc finger 2
Classification TRANSFERASE
Compound Poly [ADP-ribose] polymerase 1
Source (PARP1_HUMAN)
Sequence A:  GSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKK
MVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLK
GFSLLATEDKEALKKQLPGVKSEGKRKGDEVD
Description (1)  Poly [ADP-ribose] polymerase 1 (E.C.2.4.2.30)


Functional site

1) chain A
residue 125
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 215
source : AC1

2) chain A
residue 128
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 215
source : AC1

3) chain A
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 215
source : AC1

4) chain A
residue 162
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 215
source : AC1

5) 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_FI7

6) 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_FI8

7) 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_FI3

8) chain A
residue 177
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

9) chain A
residue 185
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

10) chain A
residue 179
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

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

12) 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_FI2

13) 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_FI2

14) 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_FI2

15) 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_FI2

16) chain A
residue 105
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

17) chain A
residue 131
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

18) 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_FI1


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