eF-site ID 2pwl-A
PDB Code 2pwl
Chain A

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Title Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549H Mutation Responsible for Crouzon Syndrome.
Classification TRANSFERASE
Compound Fibroblast growth factor receptor 2
Source Homo sapiens (Human) (FGFR2_HUMAN)
Sequence A:  ELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGIDKD
KPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN
IIHLLGACTQDGPLYVIVEYASKGNLREYLRARRPEQMTF
KDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVM
KIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVY
THQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGH
RMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI
LTLT
Description


Functional site

1) chain A
residue 625
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 303
source : AC1

2) chain A
residue 647
type
sequence L
description BINDING SITE FOR RESIDUE SO4 A 303
source : AC1

3) chain A
residue 649
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 303
source : AC1

4) chain A
residue 664
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 303
source : AC1

5) chain A
residue 737
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 304
source : AC2

6) chain A
residue 487
type
sequence L
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

7) chain A
residue 488
type
sequence G
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

8) chain A
residue 490
type
sequence G
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

9) chain A
residue 491
type
sequence A
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

10) chain A
residue 495
type
sequence V
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

11) chain A
residue 515
type
sequence A
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

12) chain A
residue 517
type
sequence K
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

13) chain A
residue 564
type
sequence V
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

14) chain A
residue 565
type
sequence E
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

15) chain A
residue 566
type
sequence Y
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

16) chain A
residue 567
type
sequence A
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

17) chain A
residue 633
type
sequence L
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

18) chain A
residue 644
type
sequence D
description BINDING SITE FOR RESIDUE ACP A 300
source : AC5

19) chain A
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

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

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

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

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

24) chain A
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

25) chain A
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

26) chain A
residue 487-517
type prosite
sequence LGEGAFGQVVMAEAVGIDKDKPKEAVTVAVK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK
source prosite : PS00107

27) chain A
residue 622-634
type prosite
sequence CIHRDLAARNVLV
description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
source prosite : PS00109


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