eF-site ID 4xi2-A
PDB Code 4xi2
Chain A

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Title Crystal Structure of an auto-inhibited form of Bruton's Tryrosine Kinase
Classification TRANSFERASE
Compound Tyrosine-protein kinase BTK
Source Mus musculus (Mouse) (BTK_MOUSE)
Sequence A:  TELKKVVALYDYMPMNANDLQLRKGEEYFILEESNLPWWR
ARDKNGQEGYIPSNYITEAEDSIEMYEWYSKHMTRSQAEQ
LLEGGFIVRDYTVSVFAKGVIRHYVVCYYLAEKHLFSTIP
ELINYHQHNSAGLISRLKYPVSKQNKNAPSTAGLGYGSWE
IDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIREGS
MSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEY
MANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQ
FLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVG
SKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKM
PYERFTNSETAEHIAQGLRLYRPHLASERVYTIMYSCWHE
KADERPSFKILLSNILDVMDE
Description


Functional site

1) chain A
residue 399
type
sequence P
description binding site for residue AU A 701
source : AC1

2) chain A
residue 464
type
sequence C
description binding site for residue AU A 701
source : AC1

3) chain A
residue 471
type
sequence F
description binding site for residue AU A 701
source : AC1

4) chain A
residue 521
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 408
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

6) chain A
residue 430
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 223
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8630736
source Swiss-Prot : SWS_FT_FI3

8) chain A
residue 408-430
type prosite
sequence LGTGQFGVVKYGKWRGQYDVAIK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGQFGVVKyGkwrgqyd...........VAIK
source prosite : PS00107

9) chain A
residue 517-529
type prosite
sequence FLHRDLAARNCLV
description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCLV
source prosite : PS00109

10) chain A
residue 344
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:17947660
source Swiss-Prot : SWS_FT_FI4

11) chain A
residue 361
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q06187
source Swiss-Prot : SWS_FT_FI5

12) chain A
residue 617
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q06187
source Swiss-Prot : SWS_FT_FI5

13) chain A
residue 551
type MOD_RES
sequence Y
description Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8629002, ECO:0007744|PubMed:17947660
source Swiss-Prot : SWS_FT_FI6

14) chain A
residue 604
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q06187
source Swiss-Prot : SWS_FT_FI7

15) chain A
residue 623
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q06187
source Swiss-Prot : SWS_FT_FI7


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