eF-site ID 4iak-A
PDB Code 4iak
Chain A

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Title Low temperature X-ray structure of cAMP dependent protein kinase A in complex with high Sr2+ concentration, ADP and phosphorylated peptide pSP20
Classification Transferase/Peptide
Compound cAMP-dependent protein kinase catalytic subunit alpha
Source Mus musculus (Mouse) (4IAK)
Sequence A:  SVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGS
FGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKR
ILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLR
RIGRFXEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL
IDQQGYIQVTDFGFAKRVKGRTWXLCGTPEYLAPEIILSK
GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG
KVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKN
HKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEE
EIRVXINEKCGKEFTEF
Description (1)  cAMP-dependent protein kinase catalytic subunit alpha (E.C.2.7.11.11), phosphorylated pseudo-substrate peptide pSP20


Functional site

1) chain A
residue 184
type
sequence D
description BINDING SITE FOR RESIDUE SR A 401
source : AC1

2) chain A
residue 171
type
sequence N
description BINDING SITE FOR RESIDUE SR A 402
source : AC2

3) chain A
residue 184
type
sequence D
description BINDING SITE FOR RESIDUE SR A 402
source : AC2

4) chain A
residue 49
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

5) chain A
residue 52
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

6) chain A
residue 53
type
sequence S
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

7) chain A
residue 57
type
sequence V
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

8) chain A
residue 70
type
sequence A
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

9) chain A
residue 72
type
sequence K
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

10) chain A
residue 104
type
sequence V
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

11) chain A
residue 120
type
sequence M
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

12) chain A
residue 121
type
sequence E
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

13) chain A
residue 122
type
sequence Y
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

14) chain A
residue 123
type
sequence V
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

15) chain A
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

16) chain A
residue 170
type
sequence E
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

17) chain A
residue 171
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

18) chain A
residue 173
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

19) chain A
residue 183
type
sequence T
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

20) chain A
residue 184
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

21) chain A
residue 327
type
sequence F
description BINDING SITE FOR RESIDUE ADP A 403
source : AC3

22) chain A
residue 64
type
sequence E
description BINDING SITE FOR RESIDUE CO3 A 404
source : AC4

23) chain A
residue 83
type
sequence K
description BINDING SITE FOR RESIDUE CO3 A 404
source : AC4

24) chain A
residue 85
type
sequence I
description BINDING SITE FOR RESIDUE CO3 A 404
source : AC4

25) chain A
residue 86
type
sequence E
description BINDING SITE FOR RESIDUE CO3 A 404
source : AC4

26) chain A
residue 49-72
type prosite
sequence LGTGSFGRVMLVKHKESGNHYAMK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhkesgnh..........YAMK
source prosite : PS00107

27) chain A
residue 162-174
type prosite
sequence LIYRDLKPENLLI
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI
source prosite : PS00108

28) chain A
residue 49
type BINDING
sequence L
description
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 72
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 121
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 168
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 48
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P17612
source Swiss-Prot : SWS_FT_FI5

33) chain A
residue 195
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P17612
source Swiss-Prot : SWS_FT_FI5

34) chain A
residue 139
type MOD_RES
sequence X
description Phosphoserine => ECO:0000269|PubMed:22323819, ECO:0000305|PubMed:8395513
source Swiss-Prot : SWS_FT_FI6

35) chain A
residue 197
type MOD_RES
sequence X
description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:22323819, ECO:0000269|PubMed:8395513, ECO:0000269|PubMed:9707564
source Swiss-Prot : SWS_FT_FI7

36) chain A
residue 330
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:21866565
source Swiss-Prot : SWS_FT_FI8

37) chain A
residue 338
type MOD_RES
sequence X
description Phosphoserine => ECO:0000305|PubMed:8395513
source Swiss-Prot : SWS_FT_FI9


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