eF-site ID 5n32-A
PDB Code 5n32
Chain A

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Title cAMP-dependent Protein Kinase A from Cricetulus griseus in complex with fragment like molecule 4-chlorobenzyl carbamimidothioate
Classification TRANSFERASE
Compound cAMP-dependent protein kinase catalytic subunit alpha
Source (A0A061IH64_CRIGR)
Sequence A:  HMGAAAAKKGXEQESVKEFLAKAKEEFLKKWESPNTAQLD
HFDRIKTLGTGSFRVMLVKHKETGNHYAMKILDKQKVVKL
KQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEY
VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDL
IYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWXLCGTP
EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ
PIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG
NLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPG
DTSNFDDYEEEEIRVXINEKCGKEFTEF
Description


Functional site

1) chain A
residue 49
type
sequence L
description binding site for residue 8K5 A 401
source : AC1

2) chain A
residue 70
type
sequence A
description binding site for residue 8K5 A 401
source : AC1

3) chain A
residue 121
type
sequence E
description binding site for residue 8K5 A 401
source : AC1

4) chain A
residue 127
type
sequence E
description binding site for residue 8K5 A 401
source : AC1

5) chain A
residue 170
type
sequence E
description binding site for residue 8K5 A 401
source : AC1

6) chain A
residue 171
type
sequence N
description binding site for residue 8K5 A 401
source : AC1

7) chain A
residue 173
type
sequence L
description binding site for residue 8K5 A 401
source : AC1

8) chain A
residue 183
type
sequence T
description binding site for residue 8K5 A 401
source : AC1

9) chain A
residue 327
type
sequence F
description binding site for residue 8K5 A 401
source : AC1

10) chain A
residue 82
type
sequence L
description binding site for residue 8K5 A 402
source : AC2

11) chain A
residue 83
type
sequence K
description binding site for residue 8K5 A 402
source : AC2

12) chain A
residue 135
type
sequence I
description binding site for residue 8K5 A 402
source : AC2

13) chain A
residue 136
type
sequence G
description binding site for residue 8K5 A 402
source : AC2

14) chain A
residue 137
type
sequence R
description binding site for residue 8K5 A 402
source : AC2

15) chain A
residue 197
type
sequence X
description binding site for residue 8K5 A 402
source : AC2

16) chain A
residue 15
type
sequence V
description binding site for residue MPD A 403
source : AC3

17) chain A
residue 100
type
sequence F
description binding site for residue MPD A 403
source : AC3

18) chain A
residue 152
type
sequence L
description binding site for residue MPD A 403
source : AC3

19) chain A
residue 155
type
sequence E
description binding site for residue MPD A 403
source : AC3

20) chain A
residue 306
type
sequence Y
description binding site for residue MPD A 403
source : AC3

21) chain A
residue 49-72
type prosite
sequence LGTGSFRVMLVKHKETGNHYAMK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........YAMK
source prosite : PS00107

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

23) chain A
residue 166
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 1
type LIPID
sequence G
description N-myristoyl glycine => ECO:0000250|UniProtKB:P17612
source Swiss-Prot : SWS_FT_FI10

25) chain A
residue 49
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 72
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 121
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 168
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 10
type MOD_RES
sequence X
description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132
source Swiss-Prot : SWS_FT_FI4

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

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

32) chain A
residue 139
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P05132
source Swiss-Prot : SWS_FT_FI6

33) chain A
residue 197
type MOD_RES
sequence X
description Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517
source Swiss-Prot : SWS_FT_FI7

34) chain A
residue 330
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P05132
source Swiss-Prot : SWS_FT_FI8

35) chain A
residue 338
type MOD_RES
sequence X
description Phosphoserine => ECO:0000250|UniProtKB:P00517
source Swiss-Prot : SWS_FT_FI9


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