eF-site ID 1xjb-B
PDB Code 1xjb
Chain B

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Title Crystal structure of human type 3 3alpha-hydroxysteroid dehydrogenase in complex with NADP(H), citrate and acetate molecules
Classification OXIDOREDUCTASE
Compound Aldo-keto reductase family 1 member C2
Source (AK1C2_HUMAN)
Sequence B:  DSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLA
IEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFY
TSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVS
VKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAK
SIGVSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRK
LLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVL
CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNV
QVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSD
EY
Description


Functional site

1) chain B
residue 55
type
sequence Y
description BINDING SITE FOR RESIDUE ACT B 6002
source : AC3

2) chain B
residue 117
type
sequence H
description BINDING SITE FOR RESIDUE ACT B 6002
source : AC3

3) chain B
residue 276
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 1004
source : AC4

4) chain B
residue 91
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 5004
source : AC5

5) chain B
residue 91
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 5004
source : AC5

6) chain B
residue 91
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 5004
source : AC5

7) chain B
residue 22
type
sequence G
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

8) chain B
residue 23
type
sequence T
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

9) chain B
residue 24
type
sequence Y
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

10) chain B
residue 50
type
sequence D
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

11) chain B
residue 55
type
sequence Y
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

12) chain B
residue 84
type
sequence K
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

13) chain B
residue 117
type
sequence H
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

14) chain B
residue 166
type
sequence S
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

15) chain B
residue 167
type
sequence N
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

16) chain B
residue 190
type
sequence Q
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

17) chain B
residue 216
type
sequence Y
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

18) chain B
residue 217
type
sequence S
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

19) chain B
residue 218
type
sequence A
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

20) chain B
residue 219
type
sequence L
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

21) chain B
residue 220
type
sequence G
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

22) chain B
residue 221
type
sequence S
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

23) chain B
residue 222
type
sequence H
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

24) chain B
residue 236
type
sequence L
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

25) chain B
residue 253
type
sequence A
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

26) chain B
residue 268
type
sequence L
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

27) chain B
residue 270
type
sequence K
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

28) chain B
residue 271
type
sequence S
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

29) chain B
residue 272
type
sequence Y
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

30) chain B
residue 276
type
sequence R
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

31) chain B
residue 279
type
sequence Q
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

32) chain B
residue 280
type
sequence N
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

33) chain B
residue 306
type
sequence L
description BINDING SITE FOR RESIDUE NAP B 5001
source : AC7

34) chain B
residue 5
type
sequence Y
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

35) chain B
residue 6
type
sequence Q
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

36) chain B
residue 17
type
sequence P
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

37) chain B
residue 18
type
sequence V
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

38) chain B
residue 19
type
sequence L
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

39) chain B
residue 45
type
sequence G
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

40) chain B
residue 46
type
sequence F
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

41) chain B
residue 47
type
sequence H
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

42) chain B
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

43) chain B
residue 284
type
sequence F
description BINDING SITE FOR RESIDUE EDO B 1003
source : AC8

44) chain B
residue 3
type
sequence S
description BINDING SITE FOR RESIDUE BME A 1005
source : BC2

45) chain B
residue 5
type
sequence Y
description BINDING SITE FOR RESIDUE BME A 1005
source : BC2

46) chain B
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE BME A 1005
source : BC2

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

48) chain B
residue 190
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 216
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 270
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338
source Swiss-Prot : SWS_FT_FI2

51) chain B
residue 20
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338
source Swiss-Prot : SWS_FT_FI2

52) chain B
residue 50
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338
source Swiss-Prot : SWS_FT_FI2

53) chain B
residue 166
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338
source Swiss-Prot : SWS_FT_FI2

54) chain B
residue 24
type BINDING
sequence Y
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

55) chain B
residue 222
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

56) chain B
residue 117
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI4

57) chain B
residue 227
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI4

58) chain B
residue 84
type SITE
sequence K
description Lowers pKa of active site Tyr => ECO:0000250
source Swiss-Prot : SWS_FT_FI5


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