eF-site ID 2v7a-B
PDB Code 2v7a
Chain B

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Title Crystal structure of the T315I Abl mutant in complex with the inhibitor PHA-739358
Classification TRANSFERASE
Compound PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL1
Source (ABL1_HUMAN)
Sequence B:  KWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTL
KEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYI
IIEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEY
LEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTX
TAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIA
TYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMR
ACWQWNPSDRPSFAEIHQAFETMFQESSIS
Description


Functional site

1) chain B
residue 248
type
sequence L
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

2) chain B
residue 250
type
sequence G
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

3) chain B
residue 269
type
sequence A
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

4) chain B
residue 271
type
sequence K
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

5) chain B
residue 316
type
sequence E
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

6) chain B
residue 317
type
sequence F
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

7) chain B
residue 318
type
sequence M
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

8) chain B
residue 319
type
sequence T
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

9) chain B
residue 321
type
sequence G
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

10) chain B
residue 367
type
sequence R
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

11) chain B
residue 370
type
sequence L
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

12) chain B
residue 381
type
sequence D
description BINDING SITE FOR RESIDUE 627 B 1504
source : AC2

13) chain B
residue 368
type
sequence N
description BINDING SITE FOR RESIDUE MG B 1505
source : AC4

14) chain B
residue 381
type
sequence D
description BINDING SITE FOR RESIDUE MG B 1505
source : AC4

15) chain B
residue 446
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P00520
source Swiss-Prot : SWS_FT_FI6

16) chain B
residue 393
type MOD_RES
sequence X
description Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036
source Swiss-Prot : SWS_FT_FI5

17) chain B
residue 363
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 248
type BINDING
sequence L
description
source Swiss-Prot : SWS_FT_FI2

19) chain B
residue 271
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 316
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

21) chain B
residue 253
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4

22) chain B
residue 257
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4

23) chain B
residue 413
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4


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