eF-site ID 6nn8-E
PDB Code 6nn8
Chain E

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Title The structure of human liver pyruvate kinase, hLPYK-S531E
Classification TRANSFERASE
Compound Pyruvate kinase PKLR
Source (KPYR_HUMAN)
Sequence E:  AFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIAT
IGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIAN
VREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQVELVK
GSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYI
DDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQV
DLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRA
ALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGD
LGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMIT
KPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVK
MQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGA
VEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRS
AQAARQVHLCRGVFPLLYREPPWADDVDRRVQFGIESGKL
RGFLRVGDLVIVVTGWRPYTNIMRVLSIS
Description


Functional site

1) chain E
residue 333
type
sequence G
description binding site for residue EDO E 601
source : AF1

2) chain E
residue 334
type
sequence K
description binding site for residue EDO E 601
source : AF1

3) chain E
residue 335
type
sequence P
description binding site for residue EDO E 601
source : AF1

4) chain E
residue 369
type
sequence D
description binding site for residue EDO E 601
source : AF1

5) chain E
residue 451
type
sequence Q
description binding site for residue EDO E 601
source : AF1

6) chain E
residue 454
type
sequence S
description binding site for residue EDO E 601
source : AF1

7) chain E
residue 455
type
sequence R
description binding site for residue EDO E 601
source : AF1

8) chain E
residue 457
type
sequence R
description binding site for residue EDO E 601
source : AF1

9) chain E
residue 478
type
sequence C
description binding site for residue EDO E 601
source : AF1

10) chain E
residue 222
type
sequence N
description binding site for residue EDO E 602
source : AF2

11) chain E
residue 223
type
sequence L
description binding site for residue EDO E 602
source : AF2

12) chain E
residue 226
type
sequence A
description binding site for residue EDO E 602
source : AF2

13) chain E
residue 256
type
sequence F
description binding site for residue EDO E 602
source : AF2

14) chain E
residue 285
type
sequence N
description binding site for residue EDO E 602
source : AF2

15) chain E
residue 312
type
sequence E
description binding site for residue EDO E 602
source : AF2

16) chain E
residue 56
type
sequence S
description binding site for residue EDO E 603
source : AF3

17) chain E
residue 58
type
sequence S
description binding site for residue EDO E 603
source : AF3

18) chain E
residue 82
type
sequence N
description binding site for residue EDO E 603
source : AF3

19) chain E
residue 476
type
sequence H
description binding site for residue EDO E 603
source : AF3

20) chain E
residue 481
type
sequence V
description binding site for residue EDO E 603
source : AF3

21) chain E
residue 482
type
sequence F
description binding site for residue EDO E 603
source : AF3

22) chain E
residue 85
type
sequence R
description binding site for residue EDO E 604
source : AF4

23) chain E
residue 282
type
sequence K
description binding site for residue EDO E 604
source : AF4

24) chain E
residue 303
type
sequence M
description binding site for residue EDO E 604
source : AF4

25) chain E
residue 305
type
sequence A
description binding site for residue EDO E 604
source : AF4

26) chain E
residue 307
type
sequence G
description binding site for residue EDO E 604
source : AF4

27) chain E
residue 308
type
sequence D
description binding site for residue EDO E 604
source : AF4

28) chain E
residue 340
type
sequence T
description binding site for residue EDO E 604
source : AF4

29) chain E
residue 278
type
sequence K
description binding site for residue EDO E 605
source : AF5

30) chain E
residue 451
type
sequence Q
description binding site for residue EDO E 605
source : AF5

31) chain E
residue 297
type
sequence E
description binding site for residue EDO E 606
source : AF6

32) chain E
residue 299
type
sequence S
description binding site for residue EDO E 606
source : AF6

33) chain E
residue 334
type
sequence K
description binding site for residue EDO E 606
source : AF6

34) chain E
residue 33
type
sequence A
description binding site for residue EDO E 607
source : AF7

35) chain E
residue 403
type
sequence H
description binding site for residue EDO E 607
source : AF7

36) chain E
residue 404
type
sequence R
description binding site for residue EDO E 607
source : AF7

37) chain E
residue 459
type
sequence R
description binding site for residue EDO E 607
source : AF7

38) chain E
residue 89
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB
source Swiss-Prot : SWS_FT_FI1

39) chain E
residue 85
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB
source Swiss-Prot : SWS_FT_FI1

40) chain E
residue 87
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

41) chain E
residue 125
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

42) chain E
residue 126
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

43) chain E
residue 282
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

44) chain E
residue 284
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

45) chain E
residue 307
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

46) chain E
residue 308
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

47) chain E
residue 340
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

48) chain E
residue 444
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

49) chain E
residue 494
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

50) chain E
residue 501
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

51) chain E
residue 528
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
source Swiss-Prot : SWS_FT_FI2

52) chain E
residue 219
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P14618
source Swiss-Prot : SWS_FT_FI3

53) chain E
residue 132
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P14618
source Swiss-Prot : SWS_FT_FI3

54) chain E
residue 282
type SITE
sequence K
description Transition state stabilizer => ECO:0000250|UniProtKB:P00549
source Swiss-Prot : SWS_FT_FI4

55) chain E
residue 261
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5


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