6RA6
Ferric murine neuroglobin Gly-loop44-47/F106A mutant
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 | 17 |
| Details | binding site for residue HEM A 201 |
| Chain | Residue |
| A | LEU31 |
| A | LEU91 |
| A | LYS94 |
| A | HIS95 |
| A | VAL98 |
| A | VAL100 |
| A | VAL108 |
| A | HOH309 |
| A | HOH329 |
| A | LEU38 |
| A | LEU41 |
| A | PHE42 |
| A | PRO58 |
| A | HIS63 |
| A | VAL67 |
| A | VAL70 |
| A | TYR87 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | ARG3 |
| A | ARG10 |
| A | ARG18 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue TRS A 203 |
| Chain | Residue |
| A | TRP13 |
| A | SER17 |
| A | PRO20 |
| A | ARG65 |
| A | ASP72 |
| A | HOH312 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 204 |
| Chain | Residue |
| A | TYR87 |
| A | HOH311 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 205 |
| Chain | Residue |
| A | HIS0 |
| A | VAL78 |
| A | HOH306 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 206 |
| Chain | Residue |
| A | ARG30 |
| A | ALA33 |
| A | TYR114 |
| A | TYR114 |
| A | LYS118 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 207 |
| Chain | Residue |
| A | ARG30 |
| A | TYR114 |
| A | TYR114 |
| A | LYS118 |
| A | LYS118 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 208 |
| Chain | Residue |
| A | ARG101 |
| A | LEU102 |
| A | SER103 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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_FI2 |
| 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 |
