eF-site ID 1xba-A
PDB Code 1xba
Chain A

click to enlarge
Title Crystal structure of apo syk tyrosine kinase domain
Classification TRANSFERASE
Compound Tyrosine-protein kinase SYK
Source (KSYK_HUMAN)
Sequence A:  VYLDRKLLTLEDKELGSGNFGTVKKGYYQMVVKTVAVKIL
PALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEM
AELGPLNKYLQQNRHVKDKNIIELVHQVSMGMKYLEESNF
VHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQT
HGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFSYGQ
KPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLCWT
YDVENRPGFAAVELRLRNYYYDVVNE
Description


Functional site

1) chain A
residue 379
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI4

2) chain A
residue 579
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI4

3) chain A
residue 384
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI5

4) chain A
residue 530
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI5

5) chain A
residue 582
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI5

6) chain A
residue 525
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI6

7) chain A
residue 546
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P48025
source Swiss-Prot : SWS_FT_FI7

8) chain A
residue 630
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI8

9) chain A
residue 377-402
type prosite
sequence LGSGNFGTVKKGYYQMVVKTVAVK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK
source prosite : PS00107

10) chain A
residue 490-502
type prosite
sequence FVHRDLAARNVLL
description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL
source prosite : PS00109

11) chain A
residue 494
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 377
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

13) chain A
residue 402
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 364
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI3

15) chain A
residue 484
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI3

16) chain A
residue 507
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI3

17) chain A
residue 526
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 629
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI3

19) chain A
residue 631
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:21469132
source Swiss-Prot : SWS_FT_FI3


Display surface

Download
Links