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

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Title GLUTATHIONE TRANSFERASE MUTANT Y115F
Classification TRANSFERASE
Compound Glutathione S-transferase YB1
Source Rattus norvegicus (Rat) (GSTM1_RAT)
Sequence A:  PMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDY
DRSQWLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLA
RKHHLCGETEEERIRADIVENQVMDNRMQLIMLCFNPDFE
KQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAY
DILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSS
RYLSTPIFSKLAQWSNK
Description


Functional site

1) chain A
residue 6
type
sequence Y
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

2) chain A
residue 7
type
sequence W
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

3) chain A
residue 12
type
sequence L
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

4) chain A
residue 42
type
sequence R
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

5) chain A
residue 45
type
sequence W
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

6) chain A
residue 49
type
sequence K
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

7) chain A
residue 58
type
sequence N
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

8) chain A
residue 59
type
sequence L
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

9) chain A
residue 60
type
sequence P
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

10) chain A
residue 71
type
sequence Q
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

11) chain A
residue 72
type
sequence S
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

12) chain A
residue 104
type
sequence M
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

13) chain A
residue 108
type
sequence M
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

14) chain A
residue 111
type
sequence I
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

15) chain A
residue 208
type
sequence F
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

16) chain A
residue 209
type
sequence S
description BINDING SITE FOR RESIDUE GPR A 5218
source : AC1

17) chain A
residue 105
type
sequence D
description BINDING SITE FOR RESIDUE GPR B 6218
source : AC2

18) chain A
residue 7
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 43
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 50
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 59
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 72
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 116
type BINDING
sequence N
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 67
type MOD_RES
sequence R
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI3

25) chain A
residue 205
type MOD_RES
sequence T
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI3

26) chain A
residue 210
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI3


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