eF-site ID 3dxb-ABCDEFGH
PDB Code 3dxb
Chain A, B, C, D, E, F, G, H

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Title Structure of the UHM domain of Puf60 fused to thioredoxin
Classification SPLICING, TRANSCRIPTION
Compound thioredoxin N-terminally fused to Puf60(UHM)
Source Homo sapiens (Human) (PUF60_HUMAN)
Sequence A:  PMSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMI
APILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTL
LLFKNGEVAATKVGALSKGQLKEFLDANLAGSAMESTVMV
LRNMVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGE
EEDAEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAE
VYDQERFDNSDLSA
B:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI
LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF
KNGEVAATKVGALSKGQLKEFLDANLAGSAMESTVMVLRN
MVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEED
AEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYD
QERFDNSDLSA
C:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI
LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF
KNGEVAATKVGALSKGQLKEFLDANLAGSAMESTVMVLRN
MVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEED
AEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYD
QERFDNSDLSA
D:  HHPMSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCK
MIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIP
TLLLFKNGEVAATKVGALSKGQLKEFLDANLAGSAMESTV
MVLRNMVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQ
GEEEDAEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVV
AEVYDQERFDNSDLSA
E:  KIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPIL
DEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFK
NGEVAATKVGALSKGQLKEFLDANLAGSAMESTVMVLRNM
VDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEEDA
EIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYDQ
ERFDNSDLSA
F:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI
LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF
KNGEVAATKVGALSKGQLKEFLDANLAGSAMESTVMVLRN
MVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEED
AEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYD
QERFDNSDLSA
G:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI
LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF
KNGEVAATKVGALSKGQLKEFLDANLAGSAMESTVMVLRN
MVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEED
AEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYD
QERFDNSDLSA
H:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI
LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF
KNGEVAATKVGALSKGQLKEFLDANLAGSAMESTVMVLRN
MVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEED
AEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYD
QERFDNSDLSA
Description


Functional site

1) chain A
residue 350
type
sequence H
description BINDING SITE FOR RESIDUE CL A 1
source : AC1

2) chain A
residue 372
type
sequence W
description BINDING SITE FOR RESIDUE CL A 1
source : AC1

3) chain E
residue 464
type
sequence R
description BINDING SITE FOR RESIDUE EDO E 557
source : AC2

4) chain E
residue 544
type
sequence Y
description BINDING SITE FOR RESIDUE EDO E 557
source : AC2

5) chain E
residue 545
type
sequence D
description BINDING SITE FOR RESIDUE EDO E 557
source : AC2

6) chain E
residue 556
type
sequence A
description BINDING SITE FOR RESIDUE EDO E 557
source : AC2

7) chain A
residue 368-386
type prosite
sequence LVDFWAEWCGPCKMIAPIL
description THIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL
source prosite : PS00194

8) chain A
residue 376
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

9) chain E
residue 379
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

10) chain F
residue 376
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

11) chain F
residue 379
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

12) chain G
residue 376
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

13) chain G
residue 379
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

14) chain H
residue 376
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

15) chain H
residue 379
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 379
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

17) chain B
residue 376
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 379
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

19) chain C
residue 376
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

20) chain C
residue 379
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

21) chain D
residue 376
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

22) chain D
residue 379
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

23) chain E
residue 376
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 370
type SITE
sequence D
description Deprotonates C-terminal active site Cys => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

25) chain B
residue 370
type SITE
sequence D
description Deprotonates C-terminal active site Cys => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

26) chain C
residue 370
type SITE
sequence D
description Deprotonates C-terminal active site Cys => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

27) chain D
residue 370
type SITE
sequence D
description Deprotonates C-terminal active site Cys => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

28) chain E
residue 370
type SITE
sequence D
description Deprotonates C-terminal active site Cys => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

29) chain F
residue 370
type SITE
sequence D
description Deprotonates C-terminal active site Cys => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

30) chain G
residue 370
type SITE
sequence D
description Deprotonates C-terminal active site Cys => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

31) chain H
residue 370
type SITE
sequence D
description Deprotonates C-terminal active site Cys => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 377
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

33) chain E
residue 378
type SITE
sequence P
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

34) chain F
residue 377
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

35) chain F
residue 378
type SITE
sequence P
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

36) chain G
residue 377
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

37) chain G
residue 378
type SITE
sequence P
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

38) chain H
residue 377
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

39) chain H
residue 378
type SITE
sequence P
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 378
type SITE
sequence P
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

41) chain B
residue 377
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

42) chain B
residue 378
type SITE
sequence P
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

43) chain C
residue 377
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

44) chain C
residue 378
type SITE
sequence P
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

45) chain D
residue 377
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

46) chain D
residue 378
type SITE
sequence P
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

47) chain E
residue 377
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

48) chain A
residue 413
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

49) chain B
residue 413
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

50) chain C
residue 413
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

51) chain D
residue 413
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

52) chain E
residue 413
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

53) chain F
residue 413
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

54) chain G
residue 413
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

55) chain H
residue 413
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4


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