eF-site ID 1a25-B
PDB Code 1a25
Chain B

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Title C2 DOMAIN FROM PROTEIN KINASE C (BETA)
Classification CALCIUM-BINDING PROTEIN
Compound PROTEIN KINASE C (BETA)
Source Rattus norvegicus (Rat) (KPCB_RAT)
Sequence B:  ERRGRIYIQAHIDREVLIVVVRDAKNLVPMDPNGLSDPYV
KLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDK
DRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFK
LLSQEEGEYFNV
Description


Functional site

1) chain B
residue 281
type
sequence E
description CA BINDING SITE.
source : CLB

2) chain B
residue 281
type
sequence E
description BINDING SITE FOR RESIDUE CA A 291
source : AC2

3) chain B
residue 281
type
sequence E
description BINDING SITE FOR RESIDUE CA A 292
source : AC3

4) chain B
residue 187
type
sequence D
description BINDING SITE FOR RESIDUE CA B 290
source : AC4

5) chain B
residue 193
type
sequence D
description BINDING SITE FOR RESIDUE CA B 290
source : AC4

6) chain B
residue 246
type
sequence D
description BINDING SITE FOR RESIDUE CA B 290
source : AC4

7) chain B
residue 247
type
sequence W
description BINDING SITE FOR RESIDUE CA B 290
source : AC4

8) chain B
residue 248
type
sequence D
description BINDING SITE FOR RESIDUE CA B 290
source : AC4

9) chain B
residue 186
type
sequence M
description BINDING SITE FOR RESIDUE CA B 291
source : AC5

10) chain B
residue 187
type
sequence D
description BINDING SITE FOR RESIDUE CA B 291
source : AC5

11) chain B
residue 246
type
sequence D
description BINDING SITE FOR RESIDUE CA B 291
source : AC5

12) chain B
residue 248
type
sequence D
description BINDING SITE FOR RESIDUE CA B 291
source : AC5

13) chain B
residue 254
type
sequence D
description BINDING SITE FOR RESIDUE CA B 291
source : AC5

14) chain B
residue 248
type
sequence D
description BINDING SITE FOR RESIDUE CA B 292
source : AC6

15) chain B
residue 251
type
sequence S
description BINDING SITE FOR RESIDUE CA B 292
source : AC6

16) chain B
residue 252
type
sequence R
description BINDING SITE FOR RESIDUE CA B 292
source : AC6

17) chain B
residue 254
type
sequence D
description BINDING SITE FOR RESIDUE CA B 292
source : AC6

18) chain B
residue 195
type
sequence Y
description BINDING SITE FOR RESIDUE PSE B 1
source : AC7

19) chain B
residue 197
type
sequence K
description BINDING SITE FOR RESIDUE PSE B 1
source : AC7

20) chain B
residue 209
type
sequence K
description BINDING SITE FOR RESIDUE PSE B 1
source : AC7

21) chain B
residue 211
type
sequence K
description BINDING SITE FOR RESIDUE PSE B 1
source : AC7

22) chain B
residue 245
type
sequence W
description BINDING SITE FOR RESIDUE PSE B 1
source : AC7

23) chain B
residue 253
type
sequence N
description BINDING SITE FOR RESIDUE PSE B 1
source : AC7

24) chain B
residue 186
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

25) chain B
residue 187
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

26) chain B
residue 193
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

27) chain B
residue 246
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 247
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

29) chain B
residue 248
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 251
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 252
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

32) chain B
residue 254
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 206
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P05771
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 250
type MOD_RES
sequence T
description Phosphothreonine; by autocatalysis => ECO:0000250
source Swiss-Prot : SWS_FT_FI3


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