|
|
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 |
138-149 |
type |
prosite |
sequence |
GNAGSRLACGVI
|
description |
SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI
|
source |
prosite : PS00332
|
|
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 |
137 |
type |
MOD_RES |
sequence |
T
|
description |
N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
20)
|
chain |
A |
residue |
7 |
type |
LIPID |
sequence |
V
|
description |
S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
|
source |
Swiss-Prot : SWS_FT_FI11
|
|
21)
|
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
|
|
22)
|
chain |
A |
residue |
64 |
type |
BINDING |
sequence |
F
|
description |
BINDING => ECO:0000269|PubMed:20727846
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
23)
|
chain |
A |
residue |
72 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000269|PubMed:20727846
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
24)
|
chain |
A |
residue |
81 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000269|PubMed:20727846
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
25)
|
chain |
A |
residue |
84 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:20727846
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
26)
|
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
|
|
27)
|
chain |
A |
residue |
4 |
type |
MOD_RES |
sequence |
A
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:P08228
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
28)
|
chain |
A |
residue |
10 |
type |
MOD_RES |
sequence |
G
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:P08228
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
29)
|
chain |
A |
residue |
92 |
type |
MOD_RES |
sequence |
D
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:P08228
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
30)
|
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
|
|
31)
|
chain |
A |
residue |
103 |
type |
MOD_RES |
sequence |
V
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
32)
|
chain |
A |
residue |
106 |
type |
MOD_RES |
sequence |
L
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P07632
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
33)
|
chain |
A |
residue |
108 |
type |
MOD_RES |
sequence |
G
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P08228
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
34)
|
chain |
A |
residue |
123 |
type |
MOD_RES |
sequence |
A
|
description |
N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
|
source |
Swiss-Prot : SWS_FT_FI9
|
|