eF-site ID 2he8-B
PDB Code 2he8
Chain B

click to enlarge
Title Crystal structure of 17alpha-hydroxysteroid dehydrogenase in its apo-form
Classification OXIDOREDUCTASE
Compound Aldo-keto reductase family 1, member C21
Source (Q9CX32_MOUSE)
Sequence B:  CHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAIDA
GFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYTSK
VWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMALKP
GEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKSIG
VSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKLLD
FCKSKDIVLVAYGVLGTQRYGGWVDQNSPVLLDEPVLGSM
AKKYNRTPALIALRYQLQRGIVVLNTSLKEERIKENMQVF
EFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDEY
Description


Functional site

1) chain B
residue 55
type
sequence Y
description BINDING SITE FOR RESIDUE ACT A 503
source : AC3

2) chain B
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE BME B 603
source : AC9

3) chain B
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE BME B 603
source : AC9

4) chain B
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE BME B 603
source : AC9

5) chain B
residue 219
type
sequence L
description BINDING SITE FOR RESIDUE GOL B 702
source : BC1

6) chain B
residue 269
type
sequence N
description BINDING SITE FOR RESIDUE GOL B 702
source : BC1

7) chain B
residue 270
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 702
source : BC1

8) chain B
residue 271
type
sequence S
description BINDING SITE FOR RESIDUE GOL B 702
source : BC1

9) chain B
residue 276
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 702
source : BC1

10) chain B
residue 279
type
sequence E
description BINDING SITE FOR RESIDUE GOL B 702
source : BC1

11) chain B
residue 280
type
sequence N
description BINDING SITE FOR RESIDUE GOL B 702
source : BC1

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

13) 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

14) 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

15) 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

16) 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

17) 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

18) 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

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

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

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


Display surface

Download
Links