eF-site ID 5c1z-A
PDB Code 5c1z
Chain A

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Title Parkin (UblR0RBR)
Classification LIGASE
Compound E3 ubiquitin-protein ligase parkin
Source Homo sapiens (Human) (PRKN2_HUMAN)
Sequence A:  MIVFVRFNSSHGFPVEVDSDTSIFQLKEVVAKRQGVPADQ
LRVIFAGKELRNDWTVQNCDLDQQSIVHIVQRPWRKGQEM
NATNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGP
SCWDDVLIPNRMSGECQSPHCPGTSAEFFFKCGAHPTSDK
ETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHVIC
LDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKE
LHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAG
LLPEPDQRKVTCEGNGFAFCRECKEAYHEGECSAVFEYRV
DERAAEQARWEATTKPCPRCHVPVEKNGGCMHMKCPQPQC
RLEWCWNCGCEWNRVCMGDHWFDV
Description


Functional site

1) chain A
residue 150
type
sequence C
description binding site for residue ZN A 501
source : AC1

2) chain A
residue 154
type
sequence C
description binding site for residue ZN A 501
source : AC1

3) chain A
residue 212
type
sequence C
description binding site for residue ZN A 501
source : AC1

4) chain A
residue 215
type
sequence H
description binding site for residue ZN A 501
source : AC1

5) chain A
residue 166
type
sequence C
description binding site for residue ZN A 502
source : AC2

6) chain A
residue 169
type
sequence C
description binding site for residue ZN A 502
source : AC2

7) chain A
residue 196
type
sequence C
description binding site for residue ZN A 502
source : AC2

8) chain A
residue 201
type
sequence C
description binding site for residue ZN A 502
source : AC2

9) chain A
residue 238
type
sequence C
description binding site for residue ZN A 503
source : AC3

10) chain A
residue 241
type
sequence C
description binding site for residue ZN A 503
source : AC3

11) chain A
residue 260
type
sequence C
description binding site for residue ZN A 503
source : AC3

12) chain A
residue 263
type
sequence C
description binding site for residue ZN A 503
source : AC3

13) chain A
residue 253
type
sequence C
description binding site for residue ZN A 504
source : AC4

14) chain A
residue 257
type
sequence H
description binding site for residue ZN A 504
source : AC4

15) chain A
residue 289
type
sequence C
description binding site for residue ZN A 504
source : AC4

16) chain A
residue 293
type
sequence C
description binding site for residue ZN A 504
source : AC4

17) chain A
residue 332
type
sequence C
description binding site for residue ZN A 505
source : AC5

18) chain A
residue 337
type
sequence C
description binding site for residue ZN A 505
source : AC5

19) chain A
residue 352
type
sequence C
description binding site for residue ZN A 505
source : AC5

20) chain A
residue 361
type
sequence G
description binding site for residue ZN A 505
source : AC5

21) chain A
residue 365
type
sequence C
description binding site for residue ZN A 506
source : AC6

22) chain A
residue 368
type
sequence C
description binding site for residue ZN A 506
source : AC6

23) chain A
residue 373
type
sequence H
description binding site for residue ZN A 506
source : AC6

24) chain A
residue 377
type
sequence C
description binding site for residue ZN A 506
source : AC6

25) chain A
residue 418
type
sequence C
description binding site for residue ZN A 507
source : AC7

26) chain A
residue 421
type
sequence C
description binding site for residue ZN A 507
source : AC7

27) chain A
residue 436
type
sequence C
description binding site for residue ZN A 507
source : AC7

28) chain A
residue 441
type
sequence C
description binding site for residue ZN A 507
source : AC7

29) chain A
residue 446
type
sequence C
description binding site for residue ZN A 508
source : AC8

30) chain A
residue 449
type
sequence C
description binding site for residue ZN A 508
source : AC8

31) chain A
residue 457
type
sequence C
description binding site for residue ZN A 508
source : AC8

32) chain A
residue 461
type
sequence H
description binding site for residue ZN A 508
source : AC8

33) chain A
residue 57
type
sequence Q
description binding site for residue SO4 A 509
source : AC9

34) chain A
residue 58
type
sequence N
description binding site for residue SO4 A 509
source : AC9

35) chain A
residue 161
type
sequence K
description binding site for residue SO4 A 509
source : AC9

36) chain A
residue 163
type
sequence R
description binding site for residue SO4 A 509
source : AC9

37) chain A
residue 211
type
sequence K
description binding site for residue SO4 A 509
source : AC9

38) chain A
residue 217
type
sequence T
description binding site for residue SO4 A 509
source : AC9

39) chain A
residue 455
type
sequence R
description binding site for residue SO4 A 509
source : AC9

40) chain A
residue 186
type
sequence V
description binding site for residue GOL A 510
source : AD1

41) chain A
residue 187
type
sequence L
description binding site for residue GOL A 510
source : AD1

42) chain A
residue 189
type
sequence P
description binding site for residue GOL A 510
source : AD1

43) chain A
residue 207
type
sequence E
description binding site for residue GOL A 510
source : AD1

44) chain A
residue 208
type
sequence F
description binding site for residue GOL A 510
source : AD1

45) chain A
residue 227
type
sequence H
description binding site for residue GOL A 511
source : AD2

46) chain A
residue 230
type
sequence A
description binding site for residue GOL A 511
source : AD2

47) chain A
residue 252
type
sequence Q
description binding site for residue GOL A 511
source : AD2

48) chain A
residue 147
type
sequence Y
description binding site for residue CL A 512
source : AD3

49) chain A
residue 183
type
sequence W
description binding site for residue CL A 512
source : AD3

50) chain A
residue 226
type
sequence L
description binding site for residue CL A 512
source : AD3

51) chain A
residue 229
type
sequence I
description binding site for residue CL A 512
source : AD3

52) chain A
residue 201-285
type ZN_FING
sequence CPGTSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCIT
CTDVRSPVLVFQCNSRHVICLDCFHLYCVTRLNDRQFVHD
PQLGY
description RING-type 0; atypical
source Swiss-Prot : SWS_FT_FI1

53) chain A
residue 277
type MOD_RES
sequence F
description Phosphothreonine => ECO:0000269|PubMed:18957282
source Swiss-Prot : SWS_FT_FI10

54) chain A
residue 429
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) => ECO:0000269|PubMed:27534820
source Swiss-Prot : SWS_FT_FI11

55) chain A
residue 298-353
type ZN_FING
sequence IKELHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGC
GAGLLPEPDQRKVTCE
description RING-type 1 => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI2

56) chain A
residue 373-437
type ZN_FING
sequence HEGECSAVFEYRVDERAAEQARWEATTKPCPRCHVPVEKN
GGCMHMKCP
description IBR-type => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI3

57) chain A
residue 298
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

58) chain A
residue 301
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

59) chain A
residue 313
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

60) chain A
residue 317
type BINDING
sequence Q
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

61) chain A
residue 320
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

62) chain A
residue 323
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

63) chain A
residue 349
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

64) chain A
residue 353
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

65) chain A
residue 433
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
source Swiss-Prot : SWS_FT_FI6

66) chain A
residue 392
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
source Swiss-Prot : SWS_FT_FI7

67) chain A
residue 397
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
source Swiss-Prot : SWS_FT_FI7

68) chain A
residue 420
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
source Swiss-Prot : SWS_FT_FI7

69) chain A
residue 425
type BINDING
sequence V
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
source Swiss-Prot : SWS_FT_FI7

70) chain A
residue 428
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
source Swiss-Prot : SWS_FT_FI7

71) chain A
residue 437
type BINDING
sequence P
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
source Swiss-Prot : SWS_FT_FI7

72) chain A
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25474007
source Swiss-Prot : SWS_FT_FI8

73) chain A
residue 235
type MOD_RES
sequence N
description Phosphothreonine; by PINK1 => ECO:0000269|PubMed:18957282
source Swiss-Prot : SWS_FT_FI9


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