eF-site ID 1l3n_21-AB
PDB Code 1l3n
Model 21
Chain A, B

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Title The Solution Structure of Reduced Dimeric Copper Zinc SOD: the Structural Effects of Dimerization
Classification OXIDOREDUCTASE
Compound superoxide dismutase [Cu-Zn]
Source Homo sapiens (Human) (SODC_HUMAN)
Sequence A:  ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
B:  ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Description


Functional site

1) chain A
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 154
source : AC1

2) chain A
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 154
source : AC1

3) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 154
source : AC1

4) chain A
residue 118
type
sequence V
description BINDING SITE FOR RESIDUE CU1 A 154
source : AC1

5) chain A
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 154
source : AC1

6) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 155
source : AC2

7) chain A
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 155
source : AC2

8) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 155
source : AC2

9) chain A
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 155
source : AC2

10) chain A
residue 136
type
sequence K
description BINDING SITE FOR RESIDUE ZN A 155
source : AC2

11) chain B
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 B 154
source : AC3

12) chain B
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 B 154
source : AC3

13) chain B
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 B 154
source : AC3

14) chain B
residue 118
type
sequence V
description BINDING SITE FOR RESIDUE CU1 B 154
source : AC3

15) chain B
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 B 154
source : AC3

16) chain B
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 155
source : AC4

17) chain B
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 155
source : AC4

18) chain B
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 155
source : AC4

19) chain B
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 155
source : AC4

20) chain A
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

24) chain B
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

25) chain B
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

27) chain B
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

28) chain A
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

29) chain B
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

30) chain A
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

31) chain B
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

32) chain A
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

35) chain A
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

39) chain B
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

41) chain B
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

42) chain A
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

43) chain A
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

44) chain A
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

45) chain B
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

46) chain B
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

47) chain B
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

48) chain A
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

49) chain B
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

50) chain A
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

51) chain B
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

52) chain A
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

53) chain B
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

54) chain A
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

55) chain B
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

56) chain A
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

57) chain B
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

58) chain A
residue 44-54
type prosite
sequence GFHVHEFGDNT
description SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHVHEfGDnT
source prosite : PS00087

59) chain A
residue 138-149
type prosite
sequence GNAGSRLACGVI
description SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI
source prosite : PS00332


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