1B4T
H48C YEAST CU(II)/ZN SUPEROXIDE DISMUTASE ROOM TEMPERATURE (298K) STRUCTURE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0005829 | cellular_component | cytosol |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0006878 | biological_process | intracellular copper ion homeostasis |
| A | 0006882 | biological_process | intracellular zinc ion homeostasis |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015680 | biological_process | protein maturation by copper ion transfer |
| A | 0016209 | molecular_function | antioxidant activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016670 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0031505 | biological_process | fungal-type cell wall organization |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050821 | biological_process | protein stabilization |
| A | 1901856 | biological_process | negative regulation of cellular respiration |
| A | 1902693 | cellular_component | superoxide dismutase complex |
| A | 1990748 | biological_process | cellular detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 154 |
| Chain | Residue |
| A | HIS46 |
| A | HIS63 |
| A | HIS120 |
| A | CL156 |
| A | HOH201 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 155 |
| Chain | Residue |
| A | HIS63 |
| A | HIS71 |
| A | HIS80 |
| A | ASP83 |
| A | LYS136 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 156 |
| Chain | Residue |
| A | HIS63 |
| A | HIS120 |
| A | ARG143 |
| A | CU154 |
| site_id | CU |
| Number of Residues | 5 |
| Details | COPPER BINDING SITE |
| Chain | Residue |
| A | CU154 |
| A | HIS46 |
| A | HIS63 |
| A | HIS120 |
| A | CL156 |
| site_id | ZN |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| A | ASP83 |
| A | ZN155 |
| A | HIS63 |
| A | HIS71 |
| A | HIS80 |
Functional Information from PROSITE/UniProt
| site_id | PS00332 |
| Number of Residues | 12 |
| Details | SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGpRpACgvI |
| Chain | Residue | Details |
| A | GLY138-ILE149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: in apo form => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675 |
| Chain | Residue | Details |
| A | ARG43 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:8652572 |
| Chain | Residue | Details |
| A | ILE47 | |
| A | GLU49 | |
| A | ALA121 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675 |
| Chain | Residue | Details |
| A | PHE64 | |
| A | GLY72 | |
| A | VAL81 | |
| A | MET84 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | PRO144 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | GLU26 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PRO39 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PHE99 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | VAL117 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | GLU132 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | GLY138 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15166219 |
| Chain | Residue | Details |
| A | PHE19 | |
| A | THR70 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| A | ARG143 | |
| A | HIS63 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| A | HIS63 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 138 |
| Chain | Residue | Details |
| A | ILE47 | metal ligand |
| A | GLU49 | metal ligand |
| A | PHE64 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | GLY72 | metal ligand |
| A | VAL81 | metal ligand |
| A | MET84 | metal ligand |
| A | ALA121 | metal ligand |
| A | PRO144 | electrostatic stabiliser, hydrogen bond donor |
