eF-site ID 1qip-C
PDB Code 1qip
Chain C

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Title HUMAN GLYOXALASE I COMPLEXED WITH S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE
Classification LYASE
Compound PROTEIN (LACTOYLGLUTATHIONE LYASE)
Source Homo sapiens (Human) (LGUL_HUMAN)
Sequence C:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF
YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK
IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI
GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD
GYWIEILNPNKMATLM
Description


Functional site

1) chain C
residue 33
type
sequence Q
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN3

2) chain C
residue 99
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN3

3) chain C
residue 126
type
sequence H
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN4

4) chain C
residue 172
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN4

5) chain C
residue 60
type
sequence C
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

6) chain C
residue 62
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

7) chain C
residue 65
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

8) chain C
residue 67
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

9) chain C
residue 69
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

10) chain C
residue 71
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

11) chain C
residue 88
type
sequence I
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

12) chain C
residue 92
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

13) chain C
residue 157
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

14) chain C
residue 160
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

15) chain C
residue 162
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

16) chain C
residue 174
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

17) chain C
residue 179
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

18) chain C
residue 183
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

19) chain C
residue 122
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
source : GH4

20) chain C
residue 37
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
source : GH3

21) chain C
residue 103
type
sequence N
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
source : GH3

22) chain C
residue 126
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 903
source : AC3

23) chain C
residue 172
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 903
source : AC3

24) chain C
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE ZN C 904
source : AC4

25) chain C
residue 99
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 904
source : AC4

26) chain C
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE GNB B 1001
source : AC5

27) chain C
residue 122
type
sequence R
description BINDING SITE FOR RESIDUE GNB D 1003
source : AC7

28) chain C
residue 157
type
sequence M
description BINDING SITE FOR RESIDUE GNB D 1003
source : AC7

29) chain C
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE GNB D 1003
source : AC7

30) chain C
residue 162
type
sequence F
description BINDING SITE FOR RESIDUE GNB D 1003
source : AC7

31) chain C
residue 179
type
sequence M
description BINDING SITE FOR RESIDUE GNB D 1003
source : AC7

32) chain C
residue 37
type
sequence R
description BINDING SITE FOR RESIDUE GNB C 1004
source : AC8

33) chain C
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE GNB C 1004
source : AC8

34) chain C
residue 67
type
sequence F
description BINDING SITE FOR RESIDUE GNB C 1004
source : AC8

35) chain C
residue 88
type
sequence I
description BINDING SITE FOR RESIDUE GNB C 1004
source : AC8

36) chain C
residue 92
type
sequence L
description BINDING SITE FOR RESIDUE GNB C 1004
source : AC8

37) chain C
residue 101
type
sequence T
description BINDING SITE FOR RESIDUE GNB C 1004
source : AC8

38) chain C
residue 103
type
sequence N
description BINDING SITE FOR RESIDUE GNB C 1004
source : AC8

39) chain C
residue 58
type
sequence Q
description BINDING SITE FOR RESIDUE BME C 204
source : BC2

40) chain C
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE BME C 204
source : BC2

41) chain C
residue 34
type catalytic
sequence T
description 32
source MCSA : MCSA3

42) chain C
residue 100
type catalytic
sequence L
description 32
source MCSA : MCSA3

43) chain C
residue 127
type catalytic
sequence I
description 32
source MCSA : MCSA3

44) chain C
residue 173
type catalytic
sequence I
description 32
source MCSA : MCSA3

45) chain C
residue 173
type ACT_SITE
sequence I
description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI1

46) chain C
residue 148
type MOD_RES
sequence F
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI10

47) chain C
residue 34
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

48) chain C
residue 100
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

49) chain C
residue 38
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI3

50) chain C
residue 104
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI3

51) chain C
residue 123
type BINDING
sequence G
description in other chain
source Swiss-Prot : SWS_FT_FI4

52) chain C
residue 157
type BINDING
sequence M
description in other chain
source Swiss-Prot : SWS_FT_FI4

53) chain C
residue 127
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

54) chain C
residue 173
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

55) chain C
residue 88
type MOD_RES
sequence I
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI7

56) chain C
residue 107
type MOD_RES
sequence E
description Phosphothreonine => ECO:0000269|PubMed:19199007
source Swiss-Prot : SWS_FT_FI8

57) chain C
residue 139
type MOD_RES
sequence K
description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
source Swiss-Prot : SWS_FT_FI9


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