2JLP
Crystal structure of human extracellular copper-zinc superoxide dismutase.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001666 | biological_process | response to hypoxia |
A | 0004784 | molecular_function | superoxide dismutase activity |
A | 0005507 | molecular_function | copper ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005796 | cellular_component | Golgi lumen |
A | 0006801 | biological_process | superoxide metabolic process |
A | 0006979 | biological_process | response to oxidative stress |
A | 0008201 | molecular_function | heparin binding |
A | 0016209 | molecular_function | antioxidant activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0046688 | biological_process | response to copper ion |
A | 0046872 | molecular_function | metal ion binding |
A | 0060090 | molecular_function | molecular adaptor activity |
A | 0062023 | cellular_component | collagen-containing extracellular matrix |
A | 0070062 | cellular_component | extracellular exosome |
A | 0097746 | biological_process | blood vessel diameter maintenance |
B | 0001666 | biological_process | response to hypoxia |
B | 0004784 | molecular_function | superoxide dismutase activity |
B | 0005507 | molecular_function | copper ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0005796 | cellular_component | Golgi lumen |
B | 0006801 | biological_process | superoxide metabolic process |
B | 0006979 | biological_process | response to oxidative stress |
B | 0008201 | molecular_function | heparin binding |
B | 0016209 | molecular_function | antioxidant activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019430 | biological_process | removal of superoxide radicals |
B | 0046688 | biological_process | response to copper ion |
B | 0046872 | molecular_function | metal ion binding |
B | 0060090 | molecular_function | molecular adaptor activity |
B | 0062023 | cellular_component | collagen-containing extracellular matrix |
B | 0070062 | cellular_component | extracellular exosome |
B | 0097746 | biological_process | blood vessel diameter maintenance |
C | 0001666 | biological_process | response to hypoxia |
C | 0004784 | molecular_function | superoxide dismutase activity |
C | 0005507 | molecular_function | copper ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005615 | cellular_component | extracellular space |
C | 0005794 | cellular_component | Golgi apparatus |
C | 0005796 | cellular_component | Golgi lumen |
C | 0006801 | biological_process | superoxide metabolic process |
C | 0006979 | biological_process | response to oxidative stress |
C | 0008201 | molecular_function | heparin binding |
C | 0016209 | molecular_function | antioxidant activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019430 | biological_process | removal of superoxide radicals |
C | 0046688 | biological_process | response to copper ion |
C | 0046872 | molecular_function | metal ion binding |
C | 0060090 | molecular_function | molecular adaptor activity |
C | 0062023 | cellular_component | collagen-containing extracellular matrix |
C | 0070062 | cellular_component | extracellular exosome |
C | 0097746 | biological_process | blood vessel diameter maintenance |
D | 0001666 | biological_process | response to hypoxia |
D | 0004784 | molecular_function | superoxide dismutase activity |
D | 0005507 | molecular_function | copper ion binding |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0005794 | cellular_component | Golgi apparatus |
D | 0005796 | cellular_component | Golgi lumen |
D | 0006801 | biological_process | superoxide metabolic process |
D | 0006979 | biological_process | response to oxidative stress |
D | 0008201 | molecular_function | heparin binding |
D | 0016209 | molecular_function | antioxidant activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019430 | biological_process | removal of superoxide radicals |
D | 0046688 | biological_process | response to copper ion |
D | 0046872 | molecular_function | metal ion binding |
D | 0060090 | molecular_function | molecular adaptor activity |
D | 0062023 | cellular_component | collagen-containing extracellular matrix |
D | 0070062 | cellular_component | extracellular exosome |
D | 0097746 | biological_process | blood vessel diameter maintenance |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 225 |
Chain | Residue |
A | HIS96 |
A | HIS98 |
A | HIS113 |
A | HIS163 |
A | HOH2128 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 226 |
Chain | Residue |
A | HIS113 |
A | HIS121 |
A | HIS124 |
A | ASP127 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU B 225 |
Chain | Residue |
B | HIS96 |
B | HIS98 |
B | HIS113 |
B | HIS163 |
B | SCN227 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 226 |
Chain | Residue |
B | HIS113 |
B | HIS121 |
B | HIS124 |
B | ASP127 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SCN B 227 |
Chain | Residue |
B | HIS98 |
B | PRO112 |
B | HIS113 |
B | HIS163 |
B | ASN180 |
B | ARG186 |
B | CU225 |
B | HOH2195 |
B | HOH2208 |
B | HOH2223 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU C 225 |
Chain | Residue |
C | HIS96 |
C | HIS98 |
C | HIS113 |
C | HIS163 |
C | SCN227 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 226 |
Chain | Residue |
C | HIS113 |
C | HIS121 |
C | HIS124 |
C | ASP127 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SCN C 227 |
Chain | Residue |
C | HIS98 |
C | PRO112 |
C | HIS113 |
C | HIS163 |
C | ASN180 |
C | ARG186 |
C | CU225 |
C | HOH2193 |
C | HOH2197 |
C | HOH2203 |
C | HOH2214 |
C | HOH2215 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU D 225 |
Chain | Residue |
D | HIS96 |
D | HIS98 |
D | HIS113 |
D | HIS163 |
D | HOH2114 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 226 |
Chain | Residue |
D | HIS113 |
D | HIS121 |
D | HIS124 |
D | ASP127 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS96 | |
B | HIS113 | |
B | HIS121 | |
B | HIS124 | |
B | ASP127 | |
B | HIS163 | |
C | HIS96 | |
C | HIS98 | |
C | HIS113 | |
C | HIS121 | |
C | HIS124 | |
A | HIS98 | |
C | ASP127 | |
C | HIS163 | |
D | HIS96 | |
D | HIS98 | |
D | HIS113 | |
D | HIS121 | |
D | HIS124 | |
D | ASP127 | |
D | HIS163 | |
A | HIS113 | |
A | HIS121 | |
A | HIS124 | |
A | ASP127 | |
A | HIS163 | |
B | HIS96 | |
B | HIS98 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | SITE: Not glycated |
Chain | Residue | Details |
A | LYS23 | |
D | LYS23 | |
D | LYS74 | |
D | LYS220 | |
A | LYS74 | |
A | LYS220 | |
B | LYS23 | |
B | LYS74 | |
B | LYS220 | |
C | LYS23 | |
C | LYS74 | |
C | LYS220 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN89 | |
B | ASN89 | |
C | ASN89 | |
D | ASN89 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:1505778 |
Chain | Residue | Details |
A | LYS211 | |
A | LYS212 | |
B | LYS211 | |
B | LYS212 | |
C | LYS211 | |
C | LYS212 | |
D | LYS211 | |
D | LYS212 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2jcw |
Chain | Residue | Details |
A | HIS113 | |
A | ARG186 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2jcw |
Chain | Residue | Details |
B | HIS113 | |
B | ARG186 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2jcw |
Chain | Residue | Details |
C | HIS113 | |
C | ARG186 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2jcw |
Chain | Residue | Details |
D | HIS113 | |
D | ARG186 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2jcw |
Chain | Residue | Details |
A | HIS113 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2jcw |
Chain | Residue | Details |
B | HIS113 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2jcw |
Chain | Residue | Details |
C | HIS113 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2jcw |
Chain | Residue | Details |
D | HIS113 |