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 | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
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 | 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 | 1 |
Details | BINDING: distal binding residue; reversible => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:15162488, ECO:0007744|PDB:1Q1F |
Chain | Residue | Details |
A | HIS64 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:15162488, ECO:0000269|PubMed:15548613, ECO:0007744|PDB:1Q1F, ECO:0007744|PDB:1W92 |
Chain | Residue | Details |
A | HIS96 |