eF-site ID 4cfh-E
PDB Code 4cfh
Chain E

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Title Structure of an active form of mammalian AMPK
Classification TRANSFERASE
Compound 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1
Source (AAKG1_RAT)
Sequence E:  NSSVYTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFAL
VTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALV
QIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSS
LIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFP
KPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHR
VSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTK
ALQHRSHYFEGVLKCYLHETLEAIINRLVEAEVHRLVVVD
EHDVVKGIVSLSDILQALVLT
Description


Functional site

1) chain E
residue 69
type
sequence R
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

2) chain E
residue 169
type
sequence K
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

3) chain E
residue 239
type
sequence I
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

4) chain E
residue 241
type
sequence S
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

5) chain E
residue 243
type
sequence F
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

6) chain E
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

7) chain E
residue 268
type
sequence R
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

8) chain E
residue 275
type
sequence V
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

9) chain E
residue 276
type
sequence L
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

10) chain E
residue 296
type
sequence V
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

11) chain E
residue 297
type
sequence H
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

12) chain E
residue 298
type
sequence R
description BINDING SITE FOR RESIDUE AMP E 1325
source : AC1

13) chain E
residue 150
type
sequence H
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

14) chain E
residue 199
type
sequence T
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

15) chain E
residue 203
type
sequence I
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

16) chain E
residue 204
type
sequence A
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

17) chain E
residue 224
type
sequence V
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

18) chain E
residue 225
type
sequence S
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

19) chain E
residue 226
type
sequence A
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

20) chain E
residue 297
type
sequence H
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

21) chain E
residue 311
type
sequence I
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

22) chain E
residue 313
type
sequence S
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

23) chain E
residue 315
type
sequence S
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

24) chain E
residue 316
type
sequence D
description BINDING SITE FOR RESIDUE AMP E 1326
source : AC2

25) chain E
residue 69
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
source Swiss-Prot : SWS_FT_FI1

26) chain E
residue 84
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
source Swiss-Prot : SWS_FT_FI1

27) chain E
residue 129
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
source Swiss-Prot : SWS_FT_FI1

28) chain E
residue 151
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
source Swiss-Prot : SWS_FT_FI1

29) chain E
residue 169
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
source Swiss-Prot : SWS_FT_FI1

30) chain E
residue 241
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
source Swiss-Prot : SWS_FT_FI1

31) chain E
residue 268
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
source Swiss-Prot : SWS_FT_FI1

32) chain E
residue 276
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
source Swiss-Prot : SWS_FT_FI1

33) chain E
residue 150
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L
source Swiss-Prot : SWS_FT_FI2

34) chain E
residue 199
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L
source Swiss-Prot : SWS_FT_FI2

35) chain E
residue 204
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L
source Swiss-Prot : SWS_FT_FI2

36) chain E
residue 225
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L
source Swiss-Prot : SWS_FT_FI2

37) chain E
residue 297
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L
source Swiss-Prot : SWS_FT_FI2

38) chain E
residue 313
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L
source Swiss-Prot : SWS_FT_FI2

39) chain E
residue 260
type MOD_RES
sequence S
description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634
source Swiss-Prot : SWS_FT_FI3

40) chain E
residue 262
type MOD_RES
sequence T
description Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634
source Swiss-Prot : SWS_FT_FI4

41) chain E
residue 269
type MOD_RES
sequence S
description Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634
source Swiss-Prot : SWS_FT_FI5


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