eF-site ID 1ba9_31-A
PDB Code 1ba9
Model 31
Chain A

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Title THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES
Classification OXIDOREDUCTASE
Compound SUPEROXIDE DISMUTASE
Source Homo sapiens (Human) (SODC_HUMAN)
Sequence A:  ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEEEDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVH
EKADDLGKGGNEQSTKTGNAGSRLACGVIGIAQ
Description


Functional site

1) chain A
residue 46
type
sequence H
description REDUCED COPPER ION (CU1+) IS COORDINATED BY THREE HISTIDINES: HIS 46, METAL COORDINATED THROUGH ND1; HIS 48, METAL COORDINATED THROUGH NE2; HIS 120 METAL COORDINATED THROUGH NE2. THE THREE MENTIONED HISTIDINES ARE PROTONATED ON THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 46 IS HIS-E, HIS 48 IS HIS-D, HIS 120 IS HIS-D. THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE ABOVE FINDINGS.
source : CU

2) chain A
residue 48
type
sequence H
description REDUCED COPPER ION (CU1+) IS COORDINATED BY THREE HISTIDINES: HIS 46, METAL COORDINATED THROUGH ND1; HIS 48, METAL COORDINATED THROUGH NE2; HIS 120 METAL COORDINATED THROUGH NE2. THE THREE MENTIONED HISTIDINES ARE PROTONATED ON THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 46 IS HIS-E, HIS 48 IS HIS-D, HIS 120 IS HIS-D. THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE ABOVE FINDINGS.
source : CU

3) chain A
residue 120
type
sequence H
description REDUCED COPPER ION (CU1+) IS COORDINATED BY THREE HISTIDINES: HIS 46, METAL COORDINATED THROUGH ND1; HIS 48, METAL COORDINATED THROUGH NE2; HIS 120 METAL COORDINATED THROUGH NE2. THE THREE MENTIONED HISTIDINES ARE PROTONATED ON THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 46 IS HIS-E, HIS 48 IS HIS-D, HIS 120 IS HIS-D. THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE ABOVE FINDINGS.
source : CU

4) chain A
residue 63
type
sequence H
description ZINC ION (ZN2+) IS COORDINATED BY THREE HISTIDINES AND BY AN ASPARTIC ACID RESIDUE. HIS 63, HIS 71 AND HIS 80 ARE METAL COORDINATED THROUGH THE ND1 ATOM. ASP 83 IS METAL COORDINATED THROUGH OD1. THE THREE HISTIDINES COORDINATED TO THE ZN ION ARE PROTONATED AT THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 63, HIS 71 AND HIS 80 ARE ALL HIS-E. THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE COORDINATION AND PROTONATION PROPERTIES OF THE HIS RESIDUES. IN ADDITION, THERE ARE SPECTROSCOPIC EVIDENCES THAT THE NON METAL COORDINATED RESIDUE HIS 43 IS PROTONATED ON BOTH N IMIDAZOLE POSITION, I.E. HIS 43 IS HIS-H.
source : ZN

5) chain A
residue 71
type
sequence H
description ZINC ION (ZN2+) IS COORDINATED BY THREE HISTIDINES AND BY AN ASPARTIC ACID RESIDUE. HIS 63, HIS 71 AND HIS 80 ARE METAL COORDINATED THROUGH THE ND1 ATOM. ASP 83 IS METAL COORDINATED THROUGH OD1. THE THREE HISTIDINES COORDINATED TO THE ZN ION ARE PROTONATED AT THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 63, HIS 71 AND HIS 80 ARE ALL HIS-E. THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE COORDINATION AND PROTONATION PROPERTIES OF THE HIS RESIDUES. IN ADDITION, THERE ARE SPECTROSCOPIC EVIDENCES THAT THE NON METAL COORDINATED RESIDUE HIS 43 IS PROTONATED ON BOTH N IMIDAZOLE POSITION, I.E. HIS 43 IS HIS-H.
source : ZN

6) chain A
residue 80
type
sequence H
description ZINC ION (ZN2+) IS COORDINATED BY THREE HISTIDINES AND BY AN ASPARTIC ACID RESIDUE. HIS 63, HIS 71 AND HIS 80 ARE METAL COORDINATED THROUGH THE ND1 ATOM. ASP 83 IS METAL COORDINATED THROUGH OD1. THE THREE HISTIDINES COORDINATED TO THE ZN ION ARE PROTONATED AT THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 63, HIS 71 AND HIS 80 ARE ALL HIS-E. THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE COORDINATION AND PROTONATION PROPERTIES OF THE HIS RESIDUES. IN ADDITION, THERE ARE SPECTROSCOPIC EVIDENCES THAT THE NON METAL COORDINATED RESIDUE HIS 43 IS PROTONATED ON BOTH N IMIDAZOLE POSITION, I.E. HIS 43 IS HIS-H.
source : ZN

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

8) chain A
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 154
source : AC1

9) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 154
source : AC1

10) chain A
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 154
source : AC1

11) chain A
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 155
source : AC2

12) chain A
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 155
source : AC2

13) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 155
source : AC2

14) chain A
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 155
source : AC2

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

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

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

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

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

20) 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

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

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

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

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

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

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

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

28) 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

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

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

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

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

33) 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

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


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