4O35
Crystal structure of carbomonoxy murine neuroglobin mutant F106W
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001666 | biological_process | response to hypoxia |
| A | 0005092 | molecular_function | GDP-dissociation inhibitor activity |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0015671 | biological_process | oxygen transport |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0031175 | biological_process | neuron projection development |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043085 | biological_process | positive regulation of catalytic activity |
| A | 0043204 | cellular_component | perikaryon |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070301 | biological_process | cellular response to hydrogen peroxide |
| A | 0071456 | biological_process | cellular response to hypoxia |
| A | 0098809 | molecular_function | nitrite reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 201 |
| Chain | Residue |
| A | LEU41 |
| A | LEU103 |
| A | TRP106 |
| A | VAL109 |
| A | TYR137 |
| A | VAL140 |
| A | CMO202 |
| A | HOH307 |
| A | HOH308 |
| A | HOH310 |
| A | HOH331 |
| A | PHE42 |
| A | HOH331 |
| A | HOH342 |
| A | HOH343 |
| A | TYR44 |
| A | HIS64 |
| A | LYS67 |
| A | LYS67 |
| A | VAL71 |
| A | LEU92 |
| A | HIS96 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO A 202 |
| Chain | Residue |
| A | PHE28 |
| A | HIS64 |
| A | HEM201 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 203 |
| Chain | Residue |
| A | SER19 |
| A | PRO20 |
| A | LEU21 |
| A | GLU22 |
| A | ARG66 |
| A | HOH326 |
| A | HOH326 |
| A | HOH377 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DIO A 204 |
| Chain | Residue |
| A | SER107 |
| A | GLY110 |
| A | GLU111 |
| A | LEU114 |
| A | SER134 |
| A | HOH380 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DIO A 205 |
| Chain | Residue |
| A | SER17 |
| A | MET69 |
| A | LEU70 |
| A | ASP73 |
| A | SER84 |
| A | HOH305 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DIO A 206 |
| Chain | Residue |
| A | LYS67 |
| A | LYS67 |
| A | LEU70 |
| A | TYR88 |
| A | TYR88 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 148 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"distal binding residue; reversible","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15162488","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q1F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15162488","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15548613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q1F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1W92","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
