eF-site ID 3fjn-A
PDB Code 3fjn
Chain A

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

11) 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

12) 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

13) 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

14) 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

15) 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

16) 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

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

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

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

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


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