eF-site ID 1ov4-A
PDB Code 1ov4
Chain A

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Title Crystal structure of human DHEA-ST complexed with androsterone
Classification TRANSFERASE
Compound Alcohol sulfotransferase
Source Homo sapiens (Human) (ST2A1_HUMAN)
Sequence A:  SDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILT
YPKSGTNWLAEILCLMHSKGDAKWIQSVPIWERSPWVESE
IGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLMR
NPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYG
SWFDHIHGWMPMREEKNFLLLSYEELKQDTGRTIEKICQF
LGKTLEPEELNLILKNSSFQSMKEYVVDKTQLSGDWKNHF
TVAQAEDFDKLFQEKMADLPRELFPWE
Description


Functional site

1) chain A
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 286
source : AC1

2) chain A
residue 45
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 286
source : AC1

3) chain A
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE SO4 A 286
source : AC1

4) chain A
residue 47
type
sequence T
description BINDING SITE FOR RESIDUE SO4 A 286
source : AC1

5) chain A
residue 48
type
sequence N
description BINDING SITE FOR RESIDUE SO4 A 286
source : AC1

6) chain A
residue 18
type
sequence F
description BINDING SITE FOR RESIDUE AOX A 287
source : AC2

7) chain A
residue 72
type
sequence W
description BINDING SITE FOR RESIDUE AOX A 287
source : AC2

8) chain A
residue 80
type
sequence S
description BINDING SITE FOR RESIDUE AOX A 287
source : AC2

9) chain A
residue 99
type
sequence H
description BINDING SITE FOR RESIDUE AOX A 287
source : AC2

10) chain A
residue 133
type
sequence F
description BINDING SITE FOR RESIDUE AOX A 287
source : AC2

11) chain A
residue 134
type
sequence W
description BINDING SITE FOR RESIDUE AOX A 287
source : AC2

12) chain A
residue 100
type ACT_SITE
sequence L
description Proton acceptor => ECO:0000269|PubMed:11988089, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1J99, ECO:0007744|PDB:1OV4
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 45
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10854859, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:1OV4, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 47
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10854859, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:1OV4, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI2

15) chain A
residue 49
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:10854859, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:1OV4, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI2

16) chain A
residue 46
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

17) chain A
residue 48
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 50
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

19) chain A
residue 122
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

20) chain A
residue 130
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 219
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

22) chain A
residue 185
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI4

23) chain A
residue 224
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI5

24) chain A
residue 252
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6


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