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

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Title CRYSTAL STRUCTURE OF THE HUMAN HYDROXYSTEROID SULFOTRANSFERASE IN THE PRESENCE OF PAP
Classification TRANSFERASE
Compound HYDROXYSTEROID SULFOTRANSFERASE
Source (ST2A1_HUMAN)
Sequence B:  DFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYP
KSGTNWLAEILCLMHSKGDAKWIQSVPIWERSPWVESEIG
YTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNP
RDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSW
FDHIHGWMPMREEKNFLLLSYEELKQDTGRTIEKICQFLG
KTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVKAQL
LRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRKLAAAL
EH
Description


Functional site

1) chain B
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

2) chain B
residue 45
type
sequence S
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

3) chain B
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

4) chain B
residue 47
type
sequence T
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

5) chain B
residue 48
type
sequence N
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

6) chain B
residue 49
type
sequence W
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

7) chain B
residue 121
type
sequence R
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

8) chain B
residue 129
type
sequence S
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

9) chain B
residue 184
type
sequence Y
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

10) chain B
residue 218
type
sequence S
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

11) chain B
residue 219
type
sequence S
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

12) chain B
residue 220
type
sequence F
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

13) chain B
residue 223
type
sequence M
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

14) chain B
residue 245
type
sequence L
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

15) chain B
residue 246
type
sequence L
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

16) chain B
residue 247
type
sequence R
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

17) chain B
residue 248
type
sequence K
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

18) chain B
residue 249
type
sequence G
description BINDING SITE FOR RESIDUE A3P B 302
source : AC1

19) chain B
residue 99
type ACT_SITE
sequence H
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

20) chain B
residue 44
type BINDING
sequence K
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

21) chain B
residue 46
type BINDING
sequence G
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

22) chain B
residue 48
type BINDING
sequence N
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

23) chain B
residue 45
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

24) chain B
residue 47
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

25) chain B
residue 49
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

26) chain B
residue 121
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

27) chain B
residue 129
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

28) chain B
residue 218
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

29) chain B
residue 247
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

30) chain B
residue 248
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI3

31) chain B
residue 249
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

32) chain B
residue 184
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI4

33) chain B
residue 223
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:4IFB
source Swiss-Prot : SWS_FT_FI5

34) chain B
residue 251
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6


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