eF-site ID 3fjn-AB
PDB Code 3fjn
Chain A, B

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Title The crystal structure of 17-alpha hydroxysteroid dehydrogenase Y224D mutant.
Classification OXIDOREDUCTASE
Compound Aldo-keto reductase family 1 member C21
Source Mus musculus (Mouse) (AK1CL_MOUSE)
Sequence A:  SKCHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAI
DAGFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYT
SKVWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMAL
KPGEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKS
IGVSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKL
LDFCKSKDIVLVAYGVLGWVDQNSPVLLDEPVLGSMAKKY
NRTPALIALRYQLQRGIVVLNTSLKEERIKENMQVFEFQL
SSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDEY
B:  SKCHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAI
DAGFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYT
SKVWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMAL
KPGEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKS
IGVSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKL
LDFCKSKDIVLVAYGVLGTQRDGGWVDQNSPVLLDEPVLG
SMAKKYNRTPALIALRYQLQRGIVVLNTSLKEERIKENMQ
VFEFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDE
Y
Description


Functional site

1) chain A
residue 55
type
sequence Y
description BINDING SITE FOR RESIDUE ACT A 601
source : AC1

2) chain A
residue 117
type
sequence H
description BINDING SITE FOR RESIDUE ACT A 601
source : AC1

3) chain A
residue 118
type
sequence Y
description BINDING SITE FOR RESIDUE ACT A 601
source : AC1

4) chain A
residue 167
type
sequence N
description BINDING SITE FOR RESIDUE ACT A 601
source : AC1

5) chain A
residue 216
type
sequence Y
description BINDING SITE FOR RESIDUE ACT A 601
source : AC1

6) chain A
residue 103
type
sequence L
description BINDING SITE FOR RESIDUE ACT A 801
source : AC2

7) chain A
residue 107
type
sequence Q
description BINDING SITE FOR RESIDUE ACT A 801
source : AC2

8) chain A
residue 108
type
sequence F
description BINDING SITE FOR RESIDUE ACT A 801
source : AC2

9) chain A
residue 246
type
sequence K
description BINDING SITE FOR RESIDUE ACT A 801
source : AC2

10) chain B
residue 219
type
sequence L
description BINDING SITE FOR RESIDUE ACT B 701
source : AC3

11) chain B
residue 253
type
sequence A
description BINDING SITE FOR RESIDUE ACT B 701
source : AC3

12) chain B
residue 269
type
sequence N
description BINDING SITE FOR RESIDUE ACT B 701
source : AC3

13) chain B
residue 276
type
sequence R
description BINDING SITE FOR RESIDUE ACT B 701
source : AC3

14) chain B
residue 279
type
sequence E
description BINDING SITE FOR RESIDUE ACT B 701
source : AC3

15) chain B
residue 280
type
sequence N
description BINDING SITE FOR RESIDUE ACT B 701
source : AC3

16) chain B
residue 55
type
sequence Y
description BINDING SITE FOR RESIDUE ACT B 901
source : AC4

17) chain B
residue 117
type
sequence H
description BINDING SITE FOR RESIDUE ACT B 901
source : AC4

18) chain B
residue 118
type
sequence Y
description BINDING SITE FOR RESIDUE ACT B 901
source : AC4

19) chain B
residue 167
type
sequence N
description BINDING SITE FOR RESIDUE ACT B 901
source : AC4

20) chain B
residue 216
type
sequence Y
description BINDING SITE FOR RESIDUE ACT B 901
source : AC4

21) chain A
residue 151-168
type prosite
sequence MEKCKDAGLTKSIGVSNF
description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglTKSIGVSNF
source prosite : PS00062

22) chain A
residue 55
type ACT_SITE
sequence Y
description Proton donor
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 55
type ACT_SITE
sequence Y
description Proton donor
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 20
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

25) chain B
residue 190
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

26) chain B
residue 216
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 270
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 50
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 166
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 190
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 216
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 270
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 20
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 50
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 166
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
source Swiss-Prot : SWS_FT_FI2

36) chain A
residue 31
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI3

37) chain A
residue 117
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI3

38) chain B
residue 31
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI3

39) chain B
residue 117
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 84
type SITE
sequence K
description Lowers pKa of active site Tyr => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

41) chain B
residue 84
type SITE
sequence K
description Lowers pKa of active site Tyr => ECO:0000250
source Swiss-Prot : SWS_FT_FI4


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