4C7U
Crystal structure of manganese superoxide dismutase from Arabidopsis thaliana
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004784 | molecular_function | superoxide dismutase activity |
A | 0006801 | biological_process | superoxide metabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004784 | molecular_function | superoxide dismutase activity |
B | 0006801 | biological_process | superoxide metabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0004784 | molecular_function | superoxide dismutase activity |
C | 0006801 | biological_process | superoxide metabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0004784 | molecular_function | superoxide dismutase activity |
D | 0006801 | biological_process | superoxide metabolic process |
D | 0046872 | molecular_function | metal ion binding |
E | 0004784 | molecular_function | superoxide dismutase activity |
E | 0006801 | biological_process | superoxide metabolic process |
E | 0046872 | molecular_function | metal ion binding |
F | 0004784 | molecular_function | superoxide dismutase activity |
F | 0006801 | biological_process | superoxide metabolic process |
F | 0046872 | molecular_function | metal ion binding |
G | 0004784 | molecular_function | superoxide dismutase activity |
G | 0006801 | biological_process | superoxide metabolic process |
G | 0046872 | molecular_function | metal ion binding |
H | 0004784 | molecular_function | superoxide dismutase activity |
H | 0006801 | biological_process | superoxide metabolic process |
H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 302 |
Chain | Residue |
A | HIS26 |
A | HIS74 |
A | ASP163 |
A | HIS167 |
A | HOH303 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 302 |
Chain | Residue |
B | HOH303 |
B | HIS26 |
B | HIS74 |
B | ASP163 |
B | HIS167 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 302 |
Chain | Residue |
C | HIS26 |
C | HIS74 |
C | ASP163 |
C | HIS167 |
C | HOH303 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 302 |
Chain | Residue |
D | HIS26 |
D | HIS74 |
D | ASP163 |
D | HIS167 |
D | HOH303 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN E 302 |
Chain | Residue |
E | HIS26 |
E | HIS74 |
E | ASP163 |
E | HIS167 |
E | HOH303 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN F 302 |
Chain | Residue |
F | HIS26 |
F | HIS74 |
F | ASP163 |
F | HIS167 |
F | HOH303 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN G 302 |
Chain | Residue |
G | HIS26 |
G | HIS74 |
G | ASP163 |
G | HIS167 |
G | HOH303 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN H 302 |
Chain | Residue |
H | HIS26 |
H | HIS74 |
H | ASP163 |
H | HIS167 |
H | HOH303 |
Functional Information from PROSITE/UniProt
site_id | PS00088 |
Number of Residues | 8 |
Details | SOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY |
Chain | Residue | Details |
A | ASP163-TYR170 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS26 | |
C | HIS74 | |
C | ASP163 | |
C | HIS167 | |
D | HIS26 | |
D | HIS74 | |
D | ASP163 | |
D | HIS167 | |
E | HIS26 | |
E | HIS74 | |
E | ASP163 | |
A | HIS74 | |
E | HIS167 | |
F | HIS26 | |
F | HIS74 | |
F | ASP163 | |
F | HIS167 | |
G | HIS26 | |
G | HIS74 | |
G | ASP163 | |
G | HIS167 | |
H | HIS26 | |
A | ASP163 | |
H | HIS74 | |
H | ASP163 | |
H | HIS167 | |
A | HIS167 | |
B | HIS26 | |
B | HIS74 | |
B | ASP163 | |
B | HIS167 | |
C | HIS26 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22092075 |
Chain | Residue | Details |
A | SER95 | |
B | SER95 | |
C | SER95 | |
D | SER95 | |
E | SER95 | |
F | SER95 | |
G | SER95 | |
H | SER95 |