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

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Title CRYSTAL STRUCTURE OF PKA IN COMPLEX WITH inhibitor.
Classification TRANSFERASE
Compound cAMP-dependent protein kinase catalytic subunit alpha
Source Bos taurus (Bovine) (IPKA_BOVIN)
Sequence A:  VKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSF
GRVMLVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRI
LQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRR
IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI
DQQGYIQVTDFGFAKRVKGRTWXLCGTPEYLAPEIILSKG
YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK
VRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKDGVNDIKNH
KWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEE
IRVXINEKCGKEFSEF
Description (1)  C-AMP-DEPENDENT PROTEIN KINASE (E.C.2.7.1.37)


Functional site

1) chain A
residue 70
type
sequence A
description binding site for residue 0RW A 401
source : AC1

2) chain A
residue 121
type
sequence E
description binding site for residue 0RW A 401
source : AC1

3) chain A
residue 122
type
sequence Y
description binding site for residue 0RW A 401
source : AC1

4) chain A
residue 123
type
sequence V
description binding site for residue 0RW A 401
source : AC1

5) chain A
residue 173
type
sequence L
description binding site for residue 0RW A 401
source : AC1

6) chain A
residue 183
type
sequence T
description binding site for residue 0RW A 401
source : AC1

7) chain A
residue 327
type
sequence F
description binding site for residue 0RW A 401
source : AC1

8) chain A
residue 166
type catalytic
sequence D
description 757
source MCSA : MCSA1

9) chain A
residue 168
type catalytic
sequence K
description 757
source MCSA : MCSA1

10) chain A
residue 171
type catalytic
sequence N
description 757
source MCSA : MCSA1

11) chain A
residue 184
type catalytic
sequence D
description 757
source MCSA : MCSA1

12) chain A
residue 201
type catalytic
sequence T
description 757
source MCSA : MCSA1

13) chain A
residue 338
type MOD_RES
sequence X
description Phosphoserine => ECO:0000269|PubMed:6262777
source Swiss-Prot : SWS_FT_FI10

14) chain A
residue 48
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P17612
source Swiss-Prot : SWS_FT_FI6

15) chain A
residue 195
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P17612
source Swiss-Prot : SWS_FT_FI6

16) chain A
residue 139
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P05132
source Swiss-Prot : SWS_FT_FI7

17) chain A
residue 197
type MOD_RES
sequence X
description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777
source Swiss-Prot : SWS_FT_FI8

18) chain A
residue 330
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P05132
source Swiss-Prot : SWS_FT_FI9

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

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

21) chain A
residue 121
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI3

22) chain A
residue 168
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI3

23) chain A
residue 49-72
type prosite
sequence LGTGSFGRVMLVKHMETGNHYAMK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK
source prosite : PS00107

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


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