eF-site ID 3w8j-ABCD
PDB Code 3w8j
Chain A, B, C, D

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Title Crystal structure of P5 a0 in a complex with Prx4 c-term
Classification OXIDOREDUCTASE/ISOMERASE
Compound Protein disulfide-isomerase A6
Source Homo sapiens (Human) (PRDX4_MOUSE)
Sequence A:  LYSSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHAQ
RLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFP
TIKIFGSNKNRPEDYQGGRTGEAIVDAALSALRQLVKDRL
G
B:  MLYSSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHA
QRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGF
PTIKIFGSNKNRPEDYQGGRTGEAIVDAALSALRQLVKDR
LG
C:  EVCPAG
D:  EVCPAG
Description (1)  Protein disulfide-isomerase A6 (E.C.5.3.4.1), C-terminal peptide from Peroxiredoxin-4 (E.C.1.11.1.15)


Functional site

1) chain A
residue 21
type
sequence Y
description BINDING SITE FOR RESIDUE K A 201
source : AC1

2) chain A
residue 49
type
sequence E
description BINDING SITE FOR RESIDUE K A 201
source : AC1

3) chain A
residue 58
type
sequence A
description BINDING SITE FOR RESIDUE K A 201
source : AC1

4) chain A
residue 62
type
sequence T
description BINDING SITE FOR RESIDUE K A 201
source : AC1

5) chain A
residue 22
type
sequence S
description BINDING SITE FOR RESIDUE K A 202
source : AC2

6) chain A
residue 25
type
sequence D
description BINDING SITE FOR RESIDUE K A 202
source : AC2

7) chain A
residue 27
type
sequence V
description BINDING SITE FOR RESIDUE K A 202
source : AC2

8) chain B
residue 40
type
sequence I
description BINDING SITE FOR RESIDUE GOL B 201
source : AC3

9) chain B
residue 109
type
sequence N
description BINDING SITE FOR RESIDUE GOL B 201
source : AC3

10) chain B
residue 121
type
sequence E
description BINDING SITE FOR RESIDUE GOL B 201
source : AC3

11) chain B
residue 122
type
sequence A
description BINDING SITE FOR RESIDUE GOL B 201
source : AC3

12) chain B
residue 125
type
sequence D
description BINDING SITE FOR RESIDUE GOL B 201
source : AC3

13) chain A
residue 41
type
sequence Q
description BINDING SITE FOR RESIDUE GOL B 202
source : AC4

14) chain B
residue 137
type
sequence D
description BINDING SITE FOR RESIDUE GOL B 202
source : AC4

15) chain B
residue 83
type
sequence A
description BINDING SITE FOR RESIDUE GOL B 203
source : AC5

16) chain B
residue 95
type
sequence V
description BINDING SITE FOR RESIDUE GOL B 203
source : AC5

17) chain B
residue 98
type
sequence F
description BINDING SITE FOR RESIDUE GOL B 203
source : AC5

18) chain D
residue 5
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 203
source : AC5

19) chain B
residue 96
type
sequence Q
description BINDING SITE FOR RESIDUE GOL B 204
source : AC6

20) chain B
residue 20
type
sequence L
description BINDING SITE FOR RESIDUE K B 205
source : AC7

21) chain B
residue 21
type
sequence Y
description BINDING SITE FOR RESIDUE K B 205
source : AC7

22) chain B
residue 49
type
sequence E
description BINDING SITE FOR RESIDUE K B 205
source : AC7

23) chain B
residue 58
type
sequence A
description BINDING SITE FOR RESIDUE K B 205
source : AC7

24) chain B
residue 62
type
sequence T
description BINDING SITE FOR RESIDUE K B 205
source : AC7

25) chain B
residue 22
type
sequence S
description BINDING SITE FOR RESIDUE K B 206
source : AC8

26) chain B
residue 23
type
sequence S
description BINDING SITE FOR RESIDUE K B 206
source : AC8

27) chain B
residue 25
type
sequence D
description BINDING SITE FOR RESIDUE K B 206
source : AC8

28) chain B
residue 27
type
sequence V
description BINDING SITE FOR RESIDUE K B 206
source : AC8

29) chain A
residue 55
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

30) chain A
residue 58
type ACT_SITE
sequence A
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 55
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

32) chain B
residue 58
type ACT_SITE
sequence A
description Nucleophile => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

33) chain A
residue 56
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 57
type SITE
sequence H
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 56
type SITE
sequence G
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 57
type SITE
sequence H
description Contributes to redox potential value => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 118
type SITE
sequence R
description Lowers pKa of C-terminal Cys of first active site => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

38) chain B
residue 118
type SITE
sequence R
description Lowers pKa of C-terminal Cys of first active site => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

39) chain A
residue 129
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI4

40) chain B
residue 129
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI4


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