eF-site ID 6ema-A
PDB Code 6ema
Chain A

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Title Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in complex with compounds RKp120 and ATP
Classification TRANSFERASE
Compound cAMP-dependent protein kinase catalytic subunit alpha
Source (6EMA)
Sequence A:  EQESVKEFLAKAKEEFLKKWESPSQNTAQLDHFDRIKTLG
TGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLN
EKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFS
HLRRIGRFXEPHARFYAAQIVLTFEYLHSLDLIYRDLKPE
NLLIDQQGYIQVTDFGFAKRVKGRTWXLCGTPEYLAPEII
LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI
VSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVND
IKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDY
EEEEIRVXINEKCGKEFTEF
Description (1)  cAMP-dependent protein kinase catalytic subunit alpha (E.C.2.7.11.11), cAMP-dependent protein kinase inhibitor


Functional site

1) 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

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

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

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

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

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

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

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

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

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

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

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

13) 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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