eF-site ID 1qh3-B
PDB Code 1qh3
Chain B

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Title HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE
Classification HYDROLASE
Compound PROTEIN (HYDROXYACYLGLUTATHIONE HYDROLASE)
Source Homo sapiens (Human) (GLO2_HUMAN)
Sequence B:  MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAA
RKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDD
RIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVS
KPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVL
GRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWA
KEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETD
PVTTMRAVRREKDQFKMPRD
Description


Functional site

1) chain B
residue 54
type
sequence H
description BINUCLEAR ZINC BINDING SITE IN B MOLECULE
source : ZNB

2) chain B
residue 56
type
sequence H
description BINUCLEAR ZINC BINDING SITE IN B MOLECULE
source : ZNB

3) chain B
residue 110
type
sequence H
description BINUCLEAR ZINC BINDING SITE IN B MOLECULE
source : ZNB

4) chain B
residue 134
type
sequence D
description BINUCLEAR ZINC BINDING SITE IN B MOLECULE
source : ZNB

5) chain B
residue 58
type
sequence D
description BINUCLEAR ZINC BINDING SITE IN B MOLECULE
source : ZNB

6) chain B
residue 59
type
sequence H
description BINUCLEAR ZINC BINDING SITE IN B MOLECULE
source : ZNB

7) chain B
residue 173
type
sequence H
description BINUCLEAR ZINC BINDING SITE IN B MOLECULE
source : ZNB

8) chain B
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 261
source : AC8

9) chain B
residue 56
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 261
source : AC8

10) chain B
residue 110
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 261
source : AC8

11) chain B
residue 134
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 261
source : AC8

12) chain B
residue 58
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 262
source : AC9

13) chain B
residue 59
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 262
source : AC9

14) chain B
residue 134
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 262
source : AC9

15) chain B
residue 173
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 262
source : AC9

16) chain B
residue 56
type
sequence H
description BINDING SITE FOR RESIDUE CAC B 469
source : BC1

17) chain B
residue 58
type
sequence D
description BINDING SITE FOR RESIDUE CAC B 469
source : BC1

18) chain B
residue 110
type
sequence H
description BINDING SITE FOR RESIDUE CAC B 469
source : BC1

19) chain B
residue 134
type
sequence D
description BINDING SITE FOR RESIDUE CAC B 469
source : BC1

20) chain B
residue 173
type
sequence H
description BINDING SITE FOR RESIDUE CAC B 469
source : BC1

21) chain B
residue 175
type
sequence Y
description BINDING SITE FOR RESIDUE CAC B 469
source : BC1

22) chain B
residue 137
type
sequence F
description BINDING SITE FOR RESIDUE ACT B 468
source : BC2

23) chain B
residue 141
type
sequence C
description BINDING SITE FOR RESIDUE ACT B 468
source : BC2

24) chain B
residue 175
type
sequence Y
description BINDING SITE FOR RESIDUE ACT B 468
source : BC2

25) chain B
residue 249
type
sequence R
description BINDING SITE FOR RESIDUE ACT B 468
source : BC2

26) chain B
residue 252
type
sequence K
description BINDING SITE FOR RESIDUE ACT B 468
source : BC2

27) chain B
residue 153
type
sequence C
description BINDING SITE FOR RESIDUE CAC B 265
source : BC3

28) chain B
residue 154
type
sequence K
description BINDING SITE FOR RESIDUE CAC B 265
source : BC3

29) chain B
residue 158
type
sequence E
description BINDING SITE FOR RESIDUE CAC B 265
source : BC3

30) chain B
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE MN B 266
source : BC4

31) chain B
residue 251
type
sequence E
description BINDING SITE FOR RESIDUE MN B 266
source : BC4

32) chain B
residue 102
type catalytic
sequence V
description 157
source MCSA : MCSA2

33) chain B
residue 104
type catalytic
sequence C
description 157
source MCSA : MCSA2

34) chain B
residue 106
type catalytic
sequence A
description 157
source MCSA : MCSA2

35) chain B
residue 107
type catalytic
sequence T
description 157
source MCSA : MCSA2

36) chain B
residue 158
type catalytic
sequence E
description 157
source MCSA : MCSA2

37) chain B
residue 182
type catalytic
sequence F
description 157
source MCSA : MCSA2

38) chain B
residue 221
type catalytic
sequence Y
description 157
source MCSA : MCSA2

39) chain B
residue 229
type MOD_RES
sequence E
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KB8
source Swiss-Prot : SWS_FT_FI3

40) chain B
residue 104
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:10508780
source Swiss-Prot : SWS_FT_FI1

41) chain B
residue 106
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:10508780
source Swiss-Prot : SWS_FT_FI1

42) chain B
residue 107
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10508780
source Swiss-Prot : SWS_FT_FI1

43) chain B
residue 158
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10508780
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 182
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:10508780
source Swiss-Prot : SWS_FT_FI1

45) chain B
residue 191
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:10508780
source Swiss-Prot : SWS_FT_FI1

46) chain B
residue 221
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10508780
source Swiss-Prot : SWS_FT_FI1

47) chain B
residue 102
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10508780
source Swiss-Prot : SWS_FT_FI1

48) chain B
residue 116
type MOD_RES
sequence C
description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KB8
source Swiss-Prot : SWS_FT_FI2


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