1F1G
Crystal structure of yeast cuznsod exposed to nitric oxide
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 | 0006825 | biological_process | copper ion transport |
| A | 0006878 | biological_process | intracellular copper ion homeostasis |
| A | 0006882 | biological_process | intracellular zinc ion homeostasis |
| A | 0008270 | molecular_function | zinc ion binding |
| 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 |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0005829 | cellular_component | cytosol |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0006825 | biological_process | copper ion transport |
| B | 0006878 | biological_process | intracellular copper ion homeostasis |
| B | 0006882 | biological_process | intracellular zinc ion homeostasis |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016209 | molecular_function | antioxidant activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016670 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0031505 | biological_process | fungal-type cell wall organization |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050821 | biological_process | protein stabilization |
| B | 1901856 | biological_process | negative regulation of cellular respiration |
| B | 1902693 | cellular_component | superoxide dismutase complex |
| B | 1990748 | biological_process | cellular detoxification |
| C | 0004784 | molecular_function | superoxide dismutase activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005758 | cellular_component | mitochondrial intermembrane space |
| C | 0005829 | cellular_component | cytosol |
| C | 0006801 | biological_process | superoxide metabolic process |
| C | 0006825 | biological_process | copper ion transport |
| C | 0006878 | biological_process | intracellular copper ion homeostasis |
| C | 0006882 | biological_process | intracellular zinc ion homeostasis |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016209 | molecular_function | antioxidant activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016670 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor |
| C | 0019430 | biological_process | removal of superoxide radicals |
| C | 0031505 | biological_process | fungal-type cell wall organization |
| C | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050821 | biological_process | protein stabilization |
| C | 1901856 | biological_process | negative regulation of cellular respiration |
| C | 1902693 | cellular_component | superoxide dismutase complex |
| C | 1990748 | biological_process | cellular detoxification |
| D | 0004784 | molecular_function | superoxide dismutase activity |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005758 | cellular_component | mitochondrial intermembrane space |
| D | 0005829 | cellular_component | cytosol |
| D | 0006801 | biological_process | superoxide metabolic process |
| D | 0006825 | biological_process | copper ion transport |
| D | 0006878 | biological_process | intracellular copper ion homeostasis |
| D | 0006882 | biological_process | intracellular zinc ion homeostasis |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016209 | molecular_function | antioxidant activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016670 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor |
| D | 0019430 | biological_process | removal of superoxide radicals |
| D | 0031505 | biological_process | fungal-type cell wall organization |
| D | 0034599 | biological_process | cellular response to oxidative stress |
| D | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050821 | biological_process | protein stabilization |
| D | 1901856 | biological_process | negative regulation of cellular respiration |
| D | 1902693 | cellular_component | superoxide dismutase complex |
| D | 1990748 | biological_process | cellular detoxification |
| E | 0004784 | molecular_function | superoxide dismutase activity |
| E | 0005507 | molecular_function | copper ion binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005758 | cellular_component | mitochondrial intermembrane space |
| E | 0005829 | cellular_component | cytosol |
| E | 0006801 | biological_process | superoxide metabolic process |
| E | 0006825 | biological_process | copper ion transport |
| E | 0006878 | biological_process | intracellular copper ion homeostasis |
| E | 0006882 | biological_process | intracellular zinc ion homeostasis |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0016209 | molecular_function | antioxidant activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016670 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor |
| E | 0019430 | biological_process | removal of superoxide radicals |
| E | 0031505 | biological_process | fungal-type cell wall organization |
| E | 0034599 | biological_process | cellular response to oxidative stress |
| E | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050821 | biological_process | protein stabilization |
| E | 1901856 | biological_process | negative regulation of cellular respiration |
| E | 1902693 | cellular_component | superoxide dismutase complex |
| E | 1990748 | biological_process | cellular detoxification |
| F | 0004784 | molecular_function | superoxide dismutase activity |
| F | 0005507 | molecular_function | copper ion binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005758 | cellular_component | mitochondrial intermembrane space |
| F | 0005829 | cellular_component | cytosol |
| F | 0006801 | biological_process | superoxide metabolic process |
| F | 0006825 | biological_process | copper ion transport |
| F | 0006878 | biological_process | intracellular copper ion homeostasis |
| F | 0006882 | biological_process | intracellular zinc ion homeostasis |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0016209 | molecular_function | antioxidant activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016670 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor |
| F | 0019430 | biological_process | removal of superoxide radicals |
| F | 0031505 | biological_process | fungal-type cell wall organization |
| F | 0034599 | biological_process | cellular response to oxidative stress |
| F | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0050821 | biological_process | protein stabilization |
| F | 1901856 | biological_process | negative regulation of cellular respiration |
| F | 1902693 | cellular_component | superoxide dismutase complex |
| F | 1990748 | biological_process | cellular detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 4001 |
| Chain | Residue |
| A | HIS46 |
| A | HIS48 |
| A | HIS63 |
| A | HIS120 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 4002 |
| Chain | Residue |
| A | HIS63 |
| A | HIS71 |
| A | HIS80 |
| A | ASP83 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 4003 |
| Chain | Residue |
| B | HIS203 |
| B | HIS218 |
| B | HIS275 |
| B | HIS201 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 4004 |
| Chain | Residue |
| B | HIS218 |
| B | HIS226 |
| B | HIS235 |
| B | ASP238 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 4005 |
| Chain | Residue |
| C | HIS356 |
| C | HIS358 |
| C | HIS373 |
| C | HIS430 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 4006 |
| Chain | Residue |
| C | HIS373 |
| C | HIS381 |
| C | HIS390 |
| C | ASP393 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU D 4007 |
| Chain | Residue |
| D | HIS511 |
| D | HIS513 |
| D | HIS528 |
| D | HIS585 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 4008 |
| Chain | Residue |
| D | HIS528 |
| D | HIS536 |
| D | HIS545 |
| D | ASP548 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU E 4009 |
| Chain | Residue |
| E | HIS666 |
| E | HIS668 |
| E | HIS683 |
| E | HIS740 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 4010 |
| Chain | Residue |
| E | HIS683 |
| E | HIS691 |
| E | HIS700 |
| E | ASP703 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU F 4011 |
| Chain | Residue |
| F | HIS821 |
| F | HIS823 |
| F | HIS838 |
| F | HIS895 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 4012 |
| Chain | Residue |
| F | HIS838 |
| F | HIS846 |
| F | HIS855 |
| F | ASP858 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 931 |
| Chain | Residue |
| A | ARG43 |
| A | HOH2205 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 932 |
| Chain | Residue |
| B | ARG198 |
| B | HOH2198 |
| B | HOH3150 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 C 933 |
| Chain | Residue |
| C | ARG353 |
| C | HOH2173 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 D 934 |
| Chain | Residue |
| D | ARG508 |
| D | HOH2216 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 E 935 |
| Chain | Residue |
| E | ARG663 |
| E | HOH2314 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 F 936 |
| Chain | Residue |
| F | ARG818 |
| F | HOH2336 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: in apo form => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675 |
| Chain | Residue | Details |
| A | ARG43 | |
| B | ARG198 | |
| C | ARG353 | |
| D | ARG508 | |
| E | ARG663 | |
| F | ARG818 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:8652572 |
| Chain | Residue | Details |
| A | ILE47 | |
| D | ILE512 | |
| D | GLU514 | |
| D | ALA586 | |
| E | ILE667 | |
| E | GLU669 | |
| E | ALA741 | |
| F | ILE822 | |
| F | GLU824 | |
| F | ALA896 | |
| A | GLU49 | |
| A | ALA121 | |
| B | ILE202 | |
| B | GLU204 | |
| B | ALA276 | |
| C | ILE357 | |
| C | GLU359 | |
| C | ALA431 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675 |
| Chain | Residue | Details |
| A | PHE64 | |
| C | GLY382 | |
| C | VAL391 | |
| C | MET394 | |
| D | PHE529 | |
| D | GLY537 | |
| D | VAL546 | |
| D | MET549 | |
| E | PHE684 | |
| E | GLY692 | |
| E | VAL701 | |
| A | GLY72 | |
| E | MET704 | |
| F | PHE839 | |
| F | GLY847 | |
| F | VAL856 | |
| F | MET859 | |
| A | VAL81 | |
| A | MET84 | |
| B | PHE219 | |
| B | GLY227 | |
| B | VAL236 | |
| B | MET239 | |
| C | PHE374 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | PRO144 | |
| B | PRO299 | |
| C | PRO454 | |
| D | PRO609 | |
| E | PRO764 | |
| F | PRO919 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | GLU26 | |
| B | GLU181 | |
| C | GLU336 | |
| D | GLU491 | |
| E | GLU646 | |
| F | GLU801 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PRO39 | |
| B | PRO194 | |
| C | PRO349 | |
| D | PRO504 | |
| E | PRO659 | |
| F | PRO814 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PHE99 | |
| B | PHE254 | |
| C | PHE409 | |
| D | PHE564 | |
| E | PHE719 | |
| F | PHE874 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | VAL117 | |
| B | VAL272 | |
| C | VAL427 | |
| D | VAL582 | |
| E | VAL737 | |
| F | VAL892 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | GLU132 | |
| B | GLU287 | |
| C | GLU442 | |
| D | GLU597 | |
| E | GLU752 | |
| F | GLU907 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | GLY138 | |
| B | GLY293 | |
| C | GLY448 | |
| D | GLY603 | |
| E | GLY758 | |
| F | GLY913 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 18 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15166219 |
| Chain | Residue | Details |
| A | PHE19 | |
| D | PHE484 | |
| D | THR535 | |
| E | PHE639 | |
| E | THR690 | |
| F | PHE794 | |
| F | THR845 | |
| A | THR70 | |
| B | PHE174 | |
| B | THR225 | |
| C | PHE329 | |
| C | THR380 |
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 | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| D | HIS528 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| E | HIS683 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| F | HIS838 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| B | ARG298 | |
| B | HIS218 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| C | ARG453 | |
| C | HIS373 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| D | HIS528 | |
| D | ARG608 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| E | HIS683 | |
| E | ARG763 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| F | HIS838 | |
| F | ARG918 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| A | HIS63 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| B | HIS218 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| C | HIS373 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 138 |
| Chain | Residue | Details |
| A | HIS46 | metal ligand |
| A | HIS48 | metal ligand |
| A | HIS63 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | HIS71 | metal ligand |
| A | HIS80 | metal ligand |
| A | ASP83 | metal ligand |
| A | HIS120 | metal ligand |
| A | ARG143 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 138 |
| Chain | Residue | Details |
| B | HIS201 | metal ligand |
| B | HIS203 | metal ligand |
| B | HIS218 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | HIS226 | metal ligand |
| B | HIS235 | metal ligand |
| B | ASP238 | metal ligand |
| B | HIS275 | metal ligand |
| B | ARG298 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 8 |
| Details | M-CSA 138 |
| Chain | Residue | Details |
| C | HIS356 | metal ligand |
| C | HIS358 | metal ligand |
| C | HIS373 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| C | HIS381 | metal ligand |
| C | HIS390 | metal ligand |
| C | ASP393 | metal ligand |
| C | HIS430 | metal ligand |
| C | ARG453 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 8 |
| Details | M-CSA 138 |
| Chain | Residue | Details |
| D | HIS511 | metal ligand |
| D | HIS513 | metal ligand |
| D | HIS528 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| D | HIS536 | metal ligand |
| D | HIS545 | metal ligand |
| D | ASP548 | metal ligand |
| D | HIS585 | metal ligand |
| D | ARG608 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA5 |
| Number of Residues | 8 |
| Details | M-CSA 138 |
| Chain | Residue | Details |
| E | HIS666 | metal ligand |
| E | HIS668 | metal ligand |
| E | HIS683 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| E | HIS691 | metal ligand |
| E | HIS700 | metal ligand |
| E | ASP703 | metal ligand |
| E | HIS740 | metal ligand |
| E | ARG763 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA6 |
| Number of Residues | 8 |
| Details | M-CSA 138 |
| Chain | Residue | Details |
| F | HIS821 | metal ligand |
| F | HIS823 | metal ligand |
| F | HIS838 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| F | HIS846 | metal ligand |
| F | HIS855 | metal ligand |
| F | ASP858 | metal ligand |
| F | HIS895 | metal ligand |
| F | ARG918 | electrostatic stabiliser, hydrogen bond donor |
