1H4O
Monoclinic form of human peroxiredoxin 5
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008379 | molecular_function | thioredoxin peroxidase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0034599 | biological_process | cellular response to oxidative stress |
B | 0008379 | molecular_function | thioredoxin peroxidase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0034599 | biological_process | cellular response to oxidative stress |
C | 0008379 | molecular_function | thioredoxin peroxidase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0034599 | biological_process | cellular response to oxidative stress |
D | 0008379 | molecular_function | thioredoxin peroxidase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0034599 | biological_process | cellular response to oxidative stress |
E | 0008379 | molecular_function | thioredoxin peroxidase activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0034599 | biological_process | cellular response to oxidative stress |
F | 0008379 | molecular_function | thioredoxin peroxidase activity |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0034599 | biological_process | cellular response to oxidative stress |
G | 0008379 | molecular_function | thioredoxin peroxidase activity |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0034599 | biological_process | cellular response to oxidative stress |
H | 0008379 | molecular_function | thioredoxin peroxidase activity |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0034599 | biological_process | cellular response to oxidative stress |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BEZ A 1162 |
Chain | Residue |
A | PRO40 |
A | THR44 |
A | PRO45 |
A | GLY46 |
A | CYS47 |
A | ARG127 |
B | ALA64 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEZ B 1162 |
Chain | Residue |
B | PRO45 |
B | GLY46 |
B | CYS47 |
B | ARG127 |
C | ALA64 |
C | HOH2092 |
B | PRO40 |
B | THR44 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BEZ C 1162 |
Chain | Residue |
C | THR44 |
C | PRO45 |
C | GLY46 |
C | CYS47 |
C | ARG127 |
C | HOH2188 |
D | LYS63 |
D | ALA64 |
D | GLY66 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BEZ D 1162 |
Chain | Residue |
D | PRO40 |
D | THR44 |
D | PRO45 |
D | GLY46 |
D | CYS47 |
D | ARG127 |
D | HOH2184 |
E | ALA64 |
E | GLY66 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BEZ E 1162 |
Chain | Residue |
E | THR44 |
E | PRO45 |
E | GLY46 |
E | CYS47 |
E | ARG127 |
E | HOH2128 |
F | LYS63 |
F | ALA64 |
F | GLY66 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BEZ F 1162 |
Chain | Residue |
F | THR44 |
F | PRO45 |
F | GLY46 |
F | CYS47 |
F | ARG127 |
F | HOH2160 |
G | LYS63 |
G | ALA64 |
G | GLY66 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEZ G 1162 |
Chain | Residue |
G | THR44 |
G | PRO45 |
G | GLY46 |
G | CYS47 |
G | PHE120 |
G | ARG127 |
G | HOH2139 |
H | ALA64 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEZ H 1162 |
Chain | Residue |
A | ALA64 |
A | HOH2090 |
H | PRO40 |
H | THR44 |
H | PRO45 |
H | GLY46 |
H | CYS47 |
H | ARG127 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Cysteine sulfenic acid (-SOH) intermediate => ECO:0000305|PubMed:10751410, ECO:0000305|PubMed:20643143 |
Chain | Residue | Details |
A | CYS47 | |
B | CYS47 | |
C | CYS47 | |
D | CYS47 | |
E | CYS47 | |
F | CYS47 | |
G | CYS47 | |
H | CYS47 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P99029 |
Chain | Residue | Details |
A | LYS22 | |
B | LYS22 | |
C | LYS22 | |
D | LYS22 | |
E | LYS22 | |
F | LYS22 | |
G | LYS22 | |
H | LYS22 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99029 |
Chain | Residue | Details |
A | LYS30 | |
B | LYS30 | |
C | LYS30 | |
D | LYS30 | |
E | LYS30 | |
F | LYS30 | |
G | LYS30 | |
H | LYS30 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P99029 |
Chain | Residue | Details |
A | LYS63 | |
B | LYS63 | |
C | LYS63 | |
D | LYS63 | |
E | LYS63 | |
F | LYS63 | |
G | LYS63 | |
H | LYS63 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9R063 |
Chain | Residue | Details |
A | SER118 | |
B | SER118 | |
C | SER118 | |
D | SER118 | |
E | SER118 | |
F | SER118 | |
G | SER118 | |
H | SER118 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99029 |
Chain | Residue | Details |
A | SER129 | |
B | SER129 | |
C | SER129 | |
D | SER129 | |
E | SER129 | |
F | SER129 | |
G | SER129 | |
H | SER129 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:31740833 |
Chain | Residue | Details |
A | CYS47 | |
B | CYS47 | |
C | CYS47 | |
D | CYS47 | |
E | CYS47 | |
F | CYS47 | |
G | CYS47 | |
H | CYS47 |