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

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Title Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome.
Classification TRANSFERASE
Compound Fibroblast growth factor receptor 2
Source Homo sapiens (Human) (FGFR2_HUMAN)
Sequence B:  GVSEYELPEDPKWEFPRDKLTLGKPLQVVMAEAVGIDKDK
PKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI
INLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGDINR
VPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNV
LVTENNVMKIADFGLARDINNYYKGRLPVKWMAPEALFDR
VYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKE
GHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD
RILTLT
Description


Functional site

1) chain B
residue 625
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 8001
source : AC3

2) chain B
residue 649
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 8001
source : AC3

3) chain B
residue 657
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 B 8001
source : AC3

4) chain B
residue 664
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 8001
source : AC3

5) chain B
residue 487
type
sequence L
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

6) chain B
residue 495
type
sequence V
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

7) chain B
residue 515
type
sequence A
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

8) chain B
residue 564
type
sequence V
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

9) chain B
residue 565
type
sequence E
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

10) chain B
residue 566
type
sequence Y
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

11) chain B
residue 567
type
sequence A
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

12) chain B
residue 571
type
sequence N
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

13) chain B
residue 630
type
sequence R
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

14) chain B
residue 633
type
sequence L
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

15) chain B
residue 644
type
sequence D
description BINDING SITE FOR RESIDUE ACP B 8002
source : AC4

16) chain B
residue 626
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208
source Swiss-Prot : SWS_FT_FI1

17) chain B
residue 466
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
source Swiss-Prot : SWS_FT_FI3

18) chain B
residue 487
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
source Swiss-Prot : SWS_FT_FI2

19) chain B
residue 517
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 565
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
source Swiss-Prot : SWS_FT_FI2

21) chain B
residue 571
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
source Swiss-Prot : SWS_FT_FI2

22) chain B
residue 656
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
source Swiss-Prot : SWS_FT_FI4

23) chain B
residue 657
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
source Swiss-Prot : SWS_FT_FI4


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