eF-site ID 6p68-C
PDB Code 6p68
Chain C

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Title Crystal structure of FGFR1-Y563C (FGFR4 surrogate) covalently bound to compound 22.
Classification TRANSFERASE
Compound Fibroblast growth factor receptor 1
Source (FGFR1_HUMAN)
Sequence C:  YELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDK
DKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHK
NIINLLGACTQDGPLYVIVECASKGNLREYLQARRPPEEQ
LSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTED
NVMKIADFGLARDIDYYKKTTNGRLPVKWMAPEALFDRIY
THQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGH
RMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI
VALTSN
Description


Functional site

1) chain C
residue 484
type
sequence L
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

2) chain C
residue 492
type
sequence V
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

3) chain C
residue 494
type
sequence L
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

4) chain C
residue 510
type
sequence K
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

5) chain C
residue 512
type
sequence A
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

6) chain C
residue 514
type
sequence K
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

7) chain C
residue 531
type
sequence E
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

8) chain C
residue 535
type
sequence M
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

9) chain C
residue 545
type
sequence I
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

10) chain C
residue 561
type
sequence V
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

11) chain C
residue 562
type
sequence E
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

12) chain C
residue 564
type
sequence A
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

13) chain C
residue 565
type
sequence S
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

14) chain C
residue 630
type
sequence L
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

15) chain C
residue 640
type
sequence A
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

16) chain C
residue 641
type
sequence D
description binding site for Di-peptide O1Y C 801 and CYS C 563
source : AC5

17) chain C
residue 623
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19224897
source Swiss-Prot : SWS_FT_FI1

18) chain C
residue 484
type BINDING
sequence L
description
source Swiss-Prot : SWS_FT_FI2

19) chain C
residue 514
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

20) chain C
residue 562
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

21) chain C
residue 568
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

22) chain C
residue 627
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

23) chain C
residue 641
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

24) chain C
residue 463
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
source Swiss-Prot : SWS_FT_FI3

25) chain C
residue 653
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701
source Swiss-Prot : SWS_FT_FI4

26) chain C
residue 654
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701
source Swiss-Prot : SWS_FT_FI4

27) chain C
residue 730
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
source Swiss-Prot : SWS_FT_FI5


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