eF-site ID 4a4c-ABC
PDB Code 4a4c
Chain A, B, C

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Title Structure of phosphoTyr371-c-Cbl-UbcH5B-ZAP-70 complex
Classification LIGASE/TRANSFERASE
Compound E3 UBIQUITIN-PROTEIN LIGASE CBL
Source (UB2D2_HUMAN)
Sequence A:  PGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDL
LPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTK
QTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKG
IFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQ
ALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRL
FQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHK
PGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQA
LIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQ
YELXCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTS
WQESEGQGCPFCRCEIKGTEPIVVDPFD
B:  SDGXTPEPA
C:  ALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPN
DSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSN
GSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP
EIARIYKDREKYNRIAREWTQKYAM
Description


Functional site

1) chain A
residue 381
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1436
source : AC1

2) chain A
residue 384
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1436
source : AC1

3) chain A
residue 401
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1436
source : AC1

4) chain A
residue 404
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1436
source : AC1

5) chain A
residue 396
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1437
source : AC2

6) chain A
residue 398
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1437
source : AC2

7) chain A
residue 416
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1437
source : AC2

8) chain A
residue 419
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1437
source : AC2

9) chain A
residue 229
type
sequence D
description BINDING SITE FOR RESIDUE CA A 1438
source : AC3

10) chain A
residue 231
type
sequence T
description BINDING SITE FOR RESIDUE CA A 1438
source : AC3

11) chain A
residue 233
type
sequence N
description BINDING SITE FOR RESIDUE CA A 1438
source : AC3

12) chain A
residue 235
type
sequence Y
description BINDING SITE FOR RESIDUE CA A 1438
source : AC3

13) chain A
residue 240
type
sequence E
description BINDING SITE FOR RESIDUE CA A 1438
source : AC3

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

15) chain C
residue 85
type ACT_SITE
sequence C
description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133
source Swiss-Prot : SWS_FT_FI1

16) 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

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

18) 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

19) 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

20) 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

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

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

23) chain C
residue 74-89
type prosite
sequence YHPNINSNGSICLDIL
description UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
source prosite : PS00183


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