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

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


Functional site

1) chain B
residue 150
type
sequence C
description binding site for residue ZN B 501
source : AD4

2) chain B
residue 154
type
sequence C
description binding site for residue ZN B 501
source : AD4

3) chain B
residue 212
type
sequence C
description binding site for residue ZN B 501
source : AD4

4) chain B
residue 215
type
sequence H
description binding site for residue ZN B 501
source : AD4

5) chain B
residue 166
type
sequence C
description binding site for residue ZN B 502
source : AD5

6) chain B
residue 169
type
sequence C
description binding site for residue ZN B 502
source : AD5

7) chain B
residue 196
type
sequence C
description binding site for residue ZN B 502
source : AD5

8) chain B
residue 201
type
sequence C
description binding site for residue ZN B 502
source : AD5

9) chain B
residue 238
type
sequence C
description binding site for residue ZN B 503
source : AD6

10) chain B
residue 241
type
sequence C
description binding site for residue ZN B 503
source : AD6

11) chain B
residue 260
type
sequence C
description binding site for residue ZN B 503
source : AD6

12) chain B
residue 263
type
sequence C
description binding site for residue ZN B 503
source : AD6

13) chain B
residue 253
type
sequence C
description binding site for residue ZN B 504
source : AD7

14) chain B
residue 257
type
sequence H
description binding site for residue ZN B 504
source : AD7

15) chain B
residue 289
type
sequence C
description binding site for residue ZN B 504
source : AD7

16) chain B
residue 293
type
sequence C
description binding site for residue ZN B 504
source : AD7

17) chain B
residue 332
type
sequence C
description binding site for residue ZN B 505
source : AD8

18) chain B
residue 337
type
sequence C
description binding site for residue ZN B 505
source : AD8

19) chain B
residue 352
type
sequence C
description binding site for residue ZN B 505
source : AD8

20) chain B
residue 361
type
sequence G
description binding site for residue ZN B 505
source : AD8

21) chain B
residue 365
type
sequence C
description binding site for residue ZN B 506
source : AD9

22) chain B
residue 368
type
sequence C
description binding site for residue ZN B 506
source : AD9

23) chain B
residue 373
type
sequence H
description binding site for residue ZN B 506
source : AD9

24) chain B
residue 377
type
sequence C
description binding site for residue ZN B 506
source : AD9

25) chain B
residue 418
type
sequence C
description binding site for residue ZN B 507
source : AE1

26) chain B
residue 421
type
sequence C
description binding site for residue ZN B 507
source : AE1

27) chain B
residue 436
type
sequence C
description binding site for residue ZN B 507
source : AE1

28) chain B
residue 441
type
sequence C
description binding site for residue ZN B 507
source : AE1

29) chain B
residue 446
type
sequence C
description binding site for residue ZN B 508
source : AE2

30) chain B
residue 449
type
sequence C
description binding site for residue ZN B 508
source : AE2

31) chain B
residue 457
type
sequence C
description binding site for residue ZN B 508
source : AE2

32) chain B
residue 461
type
sequence H
description binding site for residue ZN B 508
source : AE2

33) chain B
residue 57
type
sequence Q
description binding site for residue SO4 B 509
source : AE3

34) chain B
residue 58
type
sequence N
description binding site for residue SO4 B 509
source : AE3

35) chain B
residue 161
type
sequence K
description binding site for residue SO4 B 509
source : AE3

36) chain B
residue 163
type
sequence R
description binding site for residue SO4 B 509
source : AE3

37) chain B
residue 211
type
sequence K
description binding site for residue SO4 B 509
source : AE3

38) chain B
residue 217
type
sequence T
description binding site for residue SO4 B 509
source : AE3

39) chain B
residue 455
type
sequence R
description binding site for residue SO4 B 509
source : AE3

40) chain B
residue 227
type
sequence H
description binding site for residue GOL B 510
source : AE4

41) chain B
residue 230
type
sequence A
description binding site for residue GOL B 510
source : AE4

42) chain B
residue 250
type
sequence V
description binding site for residue GOL B 510
source : AE4

43) chain B
residue 252
type
sequence Q
description binding site for residue GOL B 510
source : AE4

44) chain B
residue 186
type
sequence V
description binding site for residue GOL B 511
source : AE5

45) chain B
residue 187
type
sequence L
description binding site for residue GOL B 511
source : AE5

46) chain B
residue 189
type
sequence P
description binding site for residue GOL B 511
source : AE5

47) chain B
residue 207
type
sequence E
description binding site for residue GOL B 511
source : AE5

48) chain B
residue 208
type
sequence F
description binding site for residue GOL B 511
source : AE5

49) chain B
residue 147
type
sequence Y
description binding site for residue CL B 512
source : AE6

50) chain B
residue 183
type
sequence W
description binding site for residue CL B 512
source : AE6

51) chain B
residue 226
type
sequence L
description binding site for residue CL B 512
source : AE6

52) chain B
residue 229
type
sequence I
description binding site for residue CL B 512
source : AE6

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

68) chain B
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

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

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

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

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

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

74) chain B
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


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