eF-site ID 5ia0-C
PDB Code 5ia0
Chain C

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Title Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with alisertib (MLN8237)
Classification TRANSFERASE
Compound Ephrin type-A receptor 2
Source (EPHA2_HUMAN)
Sequence C:  AVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTGKKEV
PVAIKTLKATEKQRVDFLGEAGIMGQFSHHNIIRLEGVIS
KYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGI
AAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSPI
RWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWEL
SNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARR
PKFADIVSILDKLIRAPDSLKTLADFDPR
Description


Functional site

1) chain C
residue 888
type
sequence D
description binding site for residue EDO A 1005
source : AC5

2) chain C
residue 890
type
sequence R
description binding site for residue EDO A 1005
source : AC5

3) chain C
residue 616
type
sequence Q
description binding site for residue EDO B 1002
source : AC9

4) chain C
residue 619
type
sequence I
description binding site for residue A5B C 1001
source : AD9

5) chain C
residue 621
type
sequence A
description binding site for residue A5B C 1001
source : AD9

6) chain C
residue 644
type
sequence A
description binding site for residue A5B C 1001
source : AD9

7) chain C
residue 646
type
sequence K
description binding site for residue A5B C 1001
source : AD9

8) chain C
residue 694
type
sequence Y
description binding site for residue A5B C 1001
source : AD9

9) chain C
residue 695
type
sequence M
description binding site for residue A5B C 1001
source : AD9

10) chain C
residue 696
type
sequence E
description binding site for residue A5B C 1001
source : AD9

11) chain C
residue 698
type
sequence G
description binding site for residue A5B C 1001
source : AD9

12) chain C
residue 702
type
sequence K
description binding site for residue A5B C 1001
source : AD9

13) chain C
residue 743
type
sequence R
description binding site for residue A5B C 1001
source : AD9

14) chain C
residue 744
type
sequence N
description binding site for residue A5B C 1001
source : AD9

15) chain C
residue 746
type
sequence L
description binding site for residue A5B C 1001
source : AD9

16) chain C
residue 756
type
sequence S
description binding site for residue A5B C 1001
source : AD9

17) chain C
residue 604
type
sequence F
description binding site for residue EDO C 1002
source : AE1

18) chain C
residue 605
type
sequence T
description binding site for residue EDO C 1002
source : AE1

19) chain C
residue 606
type
sequence T
description binding site for residue EDO C 1002
source : AE1

20) chain C
residue 668
type
sequence G
description binding site for residue EDO C 1002
source : AE1

21) chain C
residue 678
type
sequence L
description binding site for residue EDO C 1002
source : AE1

22) chain C
residue 679
type
sequence E
description binding site for residue EDO C 1002
source : AE1

23) chain C
residue 680
type
sequence G
description binding site for residue EDO C 1002
source : AE1

24) chain C
residue 617
type
sequence K
description binding site for residue EDO C 1003
source : AE2

25) chain C
residue 619
type
sequence I
description binding site for residue EDO C 1003
source : AE2

26) chain C
residue 694
type
sequence Y
description binding site for residue EDO C 1003
source : AE2

27) chain C
residue 738
type
sequence R
description binding site for residue EDO C 1004
source : AE3

28) chain C
residue 731
type
sequence A
description binding site for residue EDO C 1005
source : AE4

29) chain C
residue 863
type
sequence K
description binding site for residue EDO C 1005
source : AE4

30) chain C
residue 864
type
sequence F
description binding site for residue EDO C 1005
source : AE4

31) chain C
residue 865
type
sequence A
description binding site for residue EDO C 1005
source : AE4

32) chain C
residue 852
type
sequence Q
description binding site for residue EDO C 1006
source : AE5

33) chain C
residue 860
type
sequence R
description binding site for residue EDO C 1006
source : AE5

34) chain C
residue 735
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q03145
source Swiss-Prot : SWS_FT_FI5

35) chain C
residue 869
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19369195
source Swiss-Prot : SWS_FT_FI7

36) chain C
residue 739
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
source Swiss-Prot : SWS_FT_FI1

37) chain C
residue 619
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

38) chain C
residue 646
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

39) chain C
residue 628
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19369195
source Swiss-Prot : SWS_FT_FI3

40) chain C
residue 647
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
source Swiss-Prot : SWS_FT_FI4


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