eF-site ID 5o76-ABCDEF
PDB Code 5o76
Chain A, B, C, D, E, F

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Title Structure of phosphoY371 c-CBL in complex with ZAP70-peptide and UbV.pCBL ubiquitin variant
Classification LIGASE
Compound E3 ubiquitin-protein ligase CBL
Source Homo sapiens (Human) (5O76)
Sequence A:  TVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLP
DTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQT
ISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIF
PSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQAL
HEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQ
PWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPG
SYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALI
DGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQFE
LXCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQ
ESEGQGCPFCRCEIKGTEPIVVDPF
B:  DGXTPEP
C:  PGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDL
LPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTK
QTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKG
IFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQ
ALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRL
FQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHK
PGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQA
LIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQ
FELXCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTS
WQESEGQGCPFCRCEIKGTEPIVVDPF
D:  SDGXTPEPA
E:  SMHIFVKTGIGPIISLEVEPSDTIENVKAKIQDKEGIPPD
QQRLIFVGKQLEDGRTLSDYNIRKASYLYLVLR
F:  GSMHIFVKTGIGPIISLEVEPSDTIENVKAKIQDKEGIPP
DQQRLIFVGKQLEDGRTLSDYNIRKASYLYLVLR
Description


Functional site

1) chain A
residue 381
type
sequence C
description binding site for residue ZN A 501
source : AC1

2) chain A
residue 384
type
sequence C
description binding site for residue ZN A 501
source : AC1

3) chain A
residue 401
type
sequence C
description binding site for residue ZN A 501
source : AC1

4) chain A
residue 404
type
sequence C
description binding site for residue ZN A 501
source : AC1

5) chain A
residue 396
type
sequence C
description binding site for residue ZN A 502
source : AC2

6) chain A
residue 398
type
sequence H
description binding site for residue ZN A 502
source : AC2

7) chain A
residue 416
type
sequence C
description binding site for residue ZN A 502
source : AC2

8) chain A
residue 419
type
sequence C
description binding site for residue ZN A 502
source : AC2

9) chain A
residue 229
type
sequence D
description binding site for residue CA A 503
source : AC3

10) chain A
residue 231
type
sequence T
description binding site for residue CA A 503
source : AC3

11) chain A
residue 233
type
sequence N
description binding site for residue CA A 503
source : AC3

12) chain A
residue 235
type
sequence Y
description binding site for residue CA A 503
source : AC3

13) chain A
residue 240
type
sequence E
description binding site for residue CA A 503
source : AC3

14) chain C
residue 381
type
sequence C
description binding site for residue ZN C 501
source : AC4

15) chain C
residue 384
type
sequence C
description binding site for residue ZN C 501
source : AC4

16) chain C
residue 401
type
sequence C
description binding site for residue ZN C 501
source : AC4

17) chain C
residue 404
type
sequence C
description binding site for residue ZN C 501
source : AC4

18) chain C
residue 396
type
sequence C
description binding site for residue ZN C 502
source : AC5

19) chain C
residue 398
type
sequence H
description binding site for residue ZN C 502
source : AC5

20) chain C
residue 416
type
sequence C
description binding site for residue ZN C 502
source : AC5

21) chain C
residue 229
type
sequence D
description binding site for residue CA C 503
source : AC6

22) chain C
residue 231
type
sequence T
description binding site for residue CA C 503
source : AC6

23) chain C
residue 233
type
sequence N
description binding site for residue CA C 503
source : AC6

24) chain C
residue 235
type
sequence Y
description binding site for residue CA C 503
source : AC6

25) chain C
residue 240
type
sequence E
description binding site for residue CA C 503
source : AC6

26) chain C
residue 274
type
sequence Y
description binding site for Di-peptide GLY D 6 and PTR D 7
source : AC7

27) chain C
residue 294
type
sequence R
description binding site for Di-peptide GLY D 6 and PTR D 7
source : AC7

28) chain C
residue 296
type
sequence S
description binding site for Di-peptide GLY D 6 and PTR D 7
source : AC7

29) chain C
residue 297
type
sequence C
description binding site for Di-peptide GLY D 6 and PTR D 7
source : AC7

30) chain C
residue 298
type
sequence T
description binding site for Di-peptide GLY D 6 and PTR D 7
source : AC7

31) chain C
residue 316
type
sequence Q
description binding site for Di-peptide GLY D 6 and PTR D 7
source : AC7

32) chain D
residue 5
type
sequence D
description binding site for Di-peptide GLY D 6 and PTR D 7
source : AC7

33) chain D
residue 8
type
sequence T
description binding site for Di-peptide GLY D 6 and PTR D 7
source : AC7

34) chain C
residue 274
type
sequence Y
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

35) chain C
residue 294
type
sequence R
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

36) chain C
residue 296
type
sequence S
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

37) chain C
residue 297
type
sequence C
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

38) chain C
residue 298
type
sequence T
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

39) chain C
residue 315
type
sequence L
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

40) chain C
residue 316
type
sequence Q
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

41) chain C
residue 317
type
sequence T
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

42) chain D
residue 5
type
sequence D
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

43) chain D
residue 6
type
sequence G
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

44) chain D
residue 9
type
sequence P
description binding site for Di-peptide PTR D 7 and THR D 8
source : AC8

45) chain E
residue 27-52
type prosite
sequence KAKIQDKEGIPPDQQRLIFVGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFvGkqleD
source prosite : PS00299

46) chain A
residue 396-405
type prosite
sequence CGHLMCTSCL
description ZF_RING_1 Zinc finger RING-type signature. CgHlMCtsCL
source prosite : PS00518

47) chain D
residue 4
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:15144186
source Swiss-Prot : SWS_FT_FI1

48) chain B
residue 7
type MOD_RES
sequence X
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

49) chain C
residue 240
type MOD_RES
sequence E
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

50) chain D
residue 7
type MOD_RES
sequence X
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 233
type MOD_RES
sequence N
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 235
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

53) chain A
residue 240
type MOD_RES
sequence E
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

54) chain C
residue 229
type MOD_RES
sequence D
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

55) chain C
residue 231
type MOD_RES
sequence T
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

56) chain C
residue 233
type MOD_RES
sequence N
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

57) chain C
residue 235
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI2

58) chain A
residue 371
type MOD_RES
sequence X
description Phosphotyrosine; by INSR => ECO:0000269|PubMed:11997497
source Swiss-Prot : SWS_FT_FI4

59) chain C
residue 371
type MOD_RES
sequence X
description Phosphotyrosine; by INSR => ECO:0000269|PubMed:11997497
source Swiss-Prot : SWS_FT_FI4

60) chain A
residue 294
type BINDING
sequence R
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

61) chain C
residue 294
type BINDING
sequence R
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3


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