eF-site ID 6nn7-C
PDB Code 6nn7
Chain C

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Title The structure of human liver pyruvate kinase, hLPYK-GGG
Classification TRANSFERASE
Compound Pyruvate kinase PKLR
Source (KPYR_HUMAN)
Sequence C:  QQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPA
SRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREA
VESFAGSPYRPVAIALDTKGPEIRTGILQGGPESEVELVK
GSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYI
DDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQV
DLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRA
ALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGD
LGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMIT
KPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVK
MQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGA
VEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRS
AQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIES
GKLRGFLRVGDLVIVVTGWRGGGYTNIMRVLSIS
Description


Functional site

1) chain C
residue 421
type
sequence T
description binding site for residue FLC C 601
source : AC9

2) chain C
residue 444
type
sequence T
description binding site for residue FLC C 601
source : AC9

3) chain C
residue 445
type
sequence T
description binding site for residue FLC C 601
source : AC9

4) chain C
residue 446
type
sequence T
description binding site for residue FLC C 601
source : AC9

5) chain C
residue 448
type
sequence R
description binding site for residue FLC C 601
source : AC9

6) chain C
residue 449
type
sequence S
description binding site for residue FLC C 601
source : AC9

7) chain C
residue 534
type
sequence T
description binding site for residue FLC C 601
source : AC9

8) chain C
residue 93
type
sequence H
description binding site for residue EDO C 602
source : AD1

9) chain C
residue 247
type
sequence H
description binding site for residue EDO C 602
source : AD1

10) chain C
residue 104
type
sequence R
description binding site for residue EDO C 603
source : AD2

11) chain C
residue 122
type
sequence I
description binding site for residue EDO C 603
source : AD2

12) chain C
residue 248
type
sequence G
description binding site for residue EDO C 603
source : AD2

13) chain C
residue 249
type
sequence V
description binding site for residue EDO C 603
source : AD2

14) chain C
residue 250
type
sequence D
description binding site for residue EDO C 603
source : AD2

15) chain C
residue 473
type
sequence R
description binding site for residue EDO C 603
source : AD2

16) chain C
residue 278
type
sequence K
description binding site for residue EDO C 604
source : AD3

17) chain C
residue 451
type
sequence Q
description binding site for residue EDO C 604
source : AD3

18) chain C
residue 474
type
sequence Q
description binding site for residue EDO C 604
source : AD3

19) chain C
residue 306
type
sequence R
description binding site for residue EDO C 605
source : AD4

20) chain C
residue 318
type
sequence V
description binding site for residue EDO C 605
source : AD4

21) chain C
residue 319
type
sequence F
description binding site for residue EDO C 605
source : AD4

22) chain C
residue 322
type
sequence Q
description binding site for residue EDO C 605
source : AD4

23) chain C
residue 129
type
sequence P
description binding site for residue EDO C 606
source : AD5

24) chain C
residue 221
type
sequence V
description binding site for residue EDO C 606
source : AD5

25) chain C
residue 256
type
sequence F
description binding site for residue EDO C 606
source : AD5

26) chain C
residue 137
type
sequence Q
description binding site for residue EDO C 607
source : AD6

27) chain C
residue 165
type
sequence N
description binding site for residue EDO C 607
source : AD6

28) chain C
residue 351
type
sequence R
description binding site for residue EDO C 608
source : AD7

29) chain C
residue 85
type
sequence R
description binding site for residue GOL C 609
source : AD8

30) chain C
residue 282
type
sequence K
description binding site for residue GOL C 609
source : AD8

31) chain C
residue 305
type
sequence A
description binding site for residue GOL C 609
source : AD8

32) chain C
residue 307
type
sequence G
description binding site for residue GOL C 609
source : AD8

33) chain C
residue 308
type
sequence D
description binding site for residue GOL C 609
source : AD8

34) chain C
residue 340
type
sequence T
description binding site for residue GOL C 609
source : AD8

35) chain C
residue 528
type
sequence R
description binding site for residue GOL E 603
source : AE2

36) chain C
residue 275
type
sequence H
description binding site for residue GOL E 604
source : AE3

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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