eF-site ID 2jc6-AC
PDB Code 2jc6
Chain A, C

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Title Crystal structure of human calmodulin-dependent protein kinase 1D
Classification TRANSFERASE
Compound CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 1D
Source Homo sapiens (Human) (KCC1D_HUMAN)
Sequence A:  SWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFA
VKCIPKKASSIENEIAVLRKIKHENIVALEDIYESPNHLY
LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYL
HRMGIVHRDLKPENLLYYSQDEESKIMISPGYVAPEVLAQ
KPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILK
AEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAAR
HPWIAGDTALNKNIHESVSAQIRKNFAKSKWRQAFNAT
C:  SWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFA
VKCIPKKASIENEIAVLRKIKHENIVALEDIYESPNHLYL
VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLH
RMGIVHRDLKPENLLYYSQDEESKIMISPGYVAPEVLAQK
PYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKA
EYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARH
PWIAGDTALNKNIHESVSAQIRKNFAKSKWRQAFNAT
Description


Functional site

1) chain A
residue 29
type
sequence L
description BINDING SITE FOR RESIDUE QPP A1314
source : AC1

2) chain A
residue 99
type
sequence Q
description BINDING SITE FOR RESIDUE QPP A1314
source : AC1

3) chain A
residue 100
type
sequence L
description BINDING SITE FOR RESIDUE QPP A1314
source : AC1

4) chain A
residue 101
type
sequence V
description BINDING SITE FOR RESIDUE QPP A1314
source : AC1

5) chain A
residue 306
type
sequence W
description BINDING SITE FOR RESIDUE QPP A1314
source : AC1

6) chain A
residue 309
type
sequence A
description BINDING SITE FOR RESIDUE QPP A1314
source : AC1

7) chain C
residue 29
type
sequence L
description BINDING SITE FOR RESIDUE QPP C1314
source : AC2

8) chain C
residue 99
type
sequence Q
description BINDING SITE FOR RESIDUE QPP C1314
source : AC2

9) chain C
residue 100
type
sequence L
description BINDING SITE FOR RESIDUE QPP C1314
source : AC2

10) chain C
residue 101
type
sequence V
description BINDING SITE FOR RESIDUE QPP C1314
source : AC2

11) chain C
residue 306
type
sequence W
description BINDING SITE FOR RESIDUE QPP C1314
source : AC2

12) chain C
residue 309
type
sequence A
description BINDING SITE FOR RESIDUE QPP C1314
source : AC2

13) chain A
residue 29-57
type prosite
sequence LGTGAFSEVVLAEEKATGKLFAVKCIPKK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGAFSEVVlAeekatgklfavkc.....IPKK
source prosite : PS00107

14) chain A
residue 140-152
type prosite
sequence IVHRDLKPENLLY
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLY
source prosite : PS00108

15) chain A
residue 144
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
source Swiss-Prot : SWS_FT_FI1

16) chain C
residue 144
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 29
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

18) chain A
residue 52
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

19) chain C
residue 29
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

20) chain C
residue 52
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

21) chain A
residue 122
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

22) chain C
residue 122
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

23) chain A
residue 113
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
source Swiss-Prot : SWS_FT_FI5

24) chain C
residue 113
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
source Swiss-Prot : SWS_FT_FI5


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