1MFM
MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000302 | biological_process | response to reactive oxygen species |
A | 0000303 | biological_process | response to superoxide |
A | 0001541 | biological_process | ovarian follicle development |
A | 0001819 | biological_process | positive regulation of cytokine production |
A | 0001890 | biological_process | placenta development |
A | 0001895 | biological_process | retina homeostasis |
A | 0002262 | biological_process | myeloid cell homeostasis |
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 | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005758 | cellular_component | mitochondrial intermembrane space |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005777 | cellular_component | peroxisome |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0006801 | biological_process | superoxide metabolic process |
A | 0006879 | biological_process | intracellular iron ion homeostasis |
A | 0006915 | biological_process | apoptotic process |
A | 0006979 | biological_process | response to oxidative stress |
A | 0007283 | biological_process | spermatogenesis |
A | 0007566 | biological_process | embryo implantation |
A | 0007605 | biological_process | sensory perception of sound |
A | 0007626 | biological_process | locomotory behavior |
A | 0008089 | biological_process | anterograde axonal transport |
A | 0008090 | biological_process | retrograde axonal transport |
A | 0008217 | biological_process | regulation of blood pressure |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008340 | biological_process | determination of adult lifespan |
A | 0009408 | biological_process | response to heat |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0010467 | biological_process | gene expression |
A | 0016209 | molecular_function | antioxidant activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019226 | biological_process | transmission of nerve impulse |
A | 0019228 | biological_process | neuronal action potential |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0030346 | molecular_function | protein phosphatase 2B binding |
A | 0031267 | molecular_function | small GTPase binding |
A | 0031410 | cellular_component | cytoplasmic vesicle |
A | 0032287 | biological_process | peripheral nervous system myelin maintenance |
A | 0032839 | cellular_component | dendrite cytoplasm |
A | 0032930 | biological_process | positive regulation of superoxide anion generation |
A | 0032991 | cellular_component | protein-containing complex |
A | 0033081 | biological_process | regulation of T cell differentiation in thymus |
A | 0035234 | biological_process | ectopic germ cell programmed cell death |
A | 0040014 | biological_process | regulation of multicellular organism growth |
A | 0042542 | biological_process | response to hydrogen peroxide |
A | 0042554 | biological_process | superoxide anion generation |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043025 | cellular_component | neuronal cell body |
A | 0043065 | biological_process | positive regulation of apoptotic process |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0043087 | biological_process | regulation of GTPase activity |
A | 0043410 | biological_process | positive regulation of MAPK cascade |
A | 0043524 | biological_process | negative regulation of neuron apoptotic process |
A | 0045471 | biological_process | response to ethanol |
A | 0046620 | biological_process | regulation of organ growth |
A | 0046716 | biological_process | muscle cell cellular homeostasis |
A | 0046872 | molecular_function | metal ion binding |
A | 0048538 | biological_process | thymus development |
A | 0048678 | biological_process | response to axon injury |
A | 0050665 | biological_process | hydrogen peroxide biosynthetic process |
A | 0050728 | biological_process | negative regulation of inflammatory response |
A | 0050766 | biological_process | positive regulation of phagocytosis |
A | 0051087 | molecular_function | protein-folding chaperone binding |
A | 0051093 | biological_process | negative regulation of developmental process |
A | 0051881 | biological_process | regulation of mitochondrial membrane potential |
A | 0060047 | biological_process | heart contraction |
A | 0060052 | biological_process | neurofilament cytoskeleton organization |
A | 0060087 | biological_process | relaxation of vascular associated smooth muscle |
A | 0060088 | biological_process | auditory receptor cell stereocilium organization |
A | 0070062 | cellular_component | extracellular exosome |
A | 0072593 | biological_process | reactive oxygen species metabolic process |
A | 0099610 | biological_process | action potential initiation |
A | 1902177 | biological_process | positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway |
A | 1904115 | cellular_component | axon cytoplasm |
A | 2000242 | biological_process | negative regulation of reproductive process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 154 |
Chain | Residue |
A | HIS63 |
A | HIS71 |
A | HIS80 |
A | ASP83 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 155 |
Chain | Residue |
A | HIS46 |
A | HIS48 |
A | HIS63 |
A | HIS120 |
A | CD164 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 156 |
Chain | Residue |
A | ALA1 |
A | GLU51 |
A | ASP96 |
A | HOH178 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD A 157 |
Chain | Residue |
A | GLU121 |
A | SER142 |
A | CL165 |
A | CL166 |
A | HOH257 |
A | HOH275 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD A 158 |
Chain | Residue |
A | GLU50 |
A | ASP52 |
A | ASP90 |
A | ASP92 |
A | HOH186 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD A 159 |
Chain | Residue |
A | HIS110 |
A | GLN153 |
A | CD162 |
A | HOH210 |
A | HOH244 |
A | HOH396 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CD A 160 |
Chain | Residue |
A | GLU24 |
A | ASN53 |
A | HOH179 |
A | HOH200 |
A | HOH228 |
A | HOH319 |
A | HOH435 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 161 |
Chain | Residue |
A | ASP76 |
A | HOH206 |
A | HOH234 |
A | HOH384 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD A 162 |
Chain | Residue |
A | ASP109 |
A | HIS110 |
A | GLN153 |
A | CD159 |
A | HOH182 |
A | HOH339 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CD A 163 |
Chain | Residue |
A | ASP109 |
A | HOH209 |
A | HOH295 |
A | HOH306 |
A | HOH343 |
A | HOH376 |
A | HOH419 |
A | HOH421 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CD A 164 |
Chain | Residue |
A | HIS46 |
A | HIS48 |
A | HIS63 |
A | HIS120 |
A | CU155 |
A | HOH176 |
A | HOH224 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 165 |
Chain | Residue |
A | ARG69 |
A | GLU121 |
A | SER142 |
A | CD157 |
A | HOH322 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 166 |
Chain | Residue |
A | ARG69 |
A | LYS70 |
A | GLU78 |
A | SER142 |
A | CD157 |
site_id | CU |
Number of Residues | 4 |
Details | CU BINDING SITE COPPER ION (CU2+) IS COORDINATED BY THREE HISTIDINES: HIS 46, METAL COORDINATED THROUGH ND1; HIS 48, METAL COORDINATED THROUGH NE2; HIS 120 METAL COORDINATED THROUGH NE2. |
Chain | Residue |
A | CU155 |
A | HIS46 |
A | HIS48 |
A | HIS120 |
site_id | ZN |
Number of Residues | 5 |
Details | ZN BINDING SITE ZINC ION (ZN2+) IS COORDINATED BY THREE HISTIDINES AND BY AN ASPARTIC ACID RESIDUE. HIS 63, HIS 71 AND HIS 80 ARE METAL COORDINATED THROUGH THE ND1 ATOM. ASP 83 IS METAL COORDINATED THROUGH OD1. THE THREE HISTIDINES COORDINATED TO THE ZN ION ARE PROTONATED AT THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 63, HIS 71 AND HIS 80 ARE ALL HIS-E. |
Chain | Residue |
A | ZN154 |
A | CU155 |
A | HIS71 |
A | HIS80 |
A | ASP83 |
Functional Information from PROSITE/UniProt
site_id | PS00332 |
Number of Residues | 12 |
Details | SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI |
Chain | Residue | Details |
A | GLY138-ILE149 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 |
Chain | Residue | Details |
A | VAL47 | |
A | GLU49 | |
A | GLU121 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20727846 |
Chain | Residue | Details |
A | PHE64 | |
A | GLY72 | |
A | VAL81 | |
A | LEU84 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
A | THR2 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P08228 |
Chain | Residue | Details |
A | ALA4 | |
A | GLY10 | |
A | ASP92 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | ILE99 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | VAL103 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07632 |
Chain | Residue | Details |
A | LEU106 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P08228 |
Chain | Residue | Details |
A | GLY108 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 |
Chain | Residue | Details |
A | ALA123 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 |
Chain | Residue | Details |
A | THR137 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 |
Chain | Residue | Details |
A | VAL7 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CROSSLNK: 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836 |
Chain | Residue | Details |
A | GLY33 |
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 |