eF-site ID 6mhc-A
PDB Code 6mhc
Chain A

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Title Glutathione S-Transferase Omega 1 bound to covalent inhibitor 37
Classification Transferase/Transferase Inhibitor
Compound Glutathione S-transferase omega-1
Source (GSTO1_HUMAN)
Sequence A:  SNAMSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAER
TRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLEN
SQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMIL
ELFSKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVL
TNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTP
KLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEAC
DYGL
Description


Functional site

1) chain A
residue 29
type
sequence M
description binding site for residue JRM A 301
source : AC1

2) chain A
residue 32
type
sequence C
description binding site for residue JRM A 301
source : AC1

3) chain A
residue 56
type
sequence L
description binding site for residue JRM A 301
source : AC1

4) chain A
residue 72
type
sequence V
description binding site for residue JRM A 301
source : AC1

5) chain A
residue 128
type
sequence G
description binding site for residue JRM A 301
source : AC1

6) chain A
residue 132
type
sequence R
description binding site for residue JRM A 301
source : AC1

7) chain A
residue 229
type
sequence Y
description binding site for residue JRM A 301
source : AC1

8) chain A
residue 230
type
sequence L
description binding site for residue JRM A 301
source : AC1

9) chain A
residue 56
type
sequence L
description binding site for residue DMS A 302
source : AC2

10) chain A
residue 59
type
sequence K
description binding site for residue DMS A 302
source : AC2

11) chain A
residue 71
type
sequence L
description binding site for residue DMS A 302
source : AC2

12) chain A
residue 229
type
sequence Y
description binding site for residue DMS A 302
source : AC2

13) chain A
residue 43
type
sequence K
description binding site for residue PEG A 303
source : AC3

14) chain A
residue 211
type
sequence T
description binding site for residue PEG A 303
source : AC3

15) chain A
residue 34
type
sequence F
description binding site for residue MES A 304
source : AC4

16) chain A
residue 85
type
sequence E
description binding site for residue MES A 304
source : AC4

17) chain A
residue 86
type
sequence S
description binding site for residue MES A 304
source : AC4

18) chain A
residue 118
type
sequence E
description binding site for residue MES B 304
source : AC7

19) chain A
residue 32
type ACT_SITE
sequence C
description Nucleophile => ECO:0000269|PubMed:10783391
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 59
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529
source Swiss-Prot : SWS_FT_FI2

21) chain A
residue 72
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 85
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529
source Swiss-Prot : SWS_FT_FI2

23) chain A
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI3

24) chain A
residue 57
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

25) chain A
residue 143
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

26) chain A
residue 148
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

27) chain A
residue 152
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

28) chain A
residue 129
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5


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