3AG0
Crystal structure of carbonmonoxy human cytoglobin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001666 | biological_process | response to hypoxia |
| A | 0004096 | molecular_function | catalase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0010764 | biological_process | negative regulation of fibroblast migration |
| A | 0015671 | biological_process | oxygen transport |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019395 | biological_process | fatty acid oxidation |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0032966 | biological_process | negative regulation of collagen biosynthetic process |
| A | 0043005 | cellular_component | neuron projection |
| A | 0043025 | cellular_component | neuronal cell body |
| A | 0046210 | biological_process | nitric oxide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047888 | molecular_function | fatty acid peroxidase activity |
| A | 0070025 | molecular_function | carbon monoxide binding |
| A | 0098809 | molecular_function | nitrite reductase activity |
| A | 0141118 | molecular_function | nitric oxide dioxygenase activity, heme protein as donor |
| A | 2000490 | biological_process | negative regulation of hepatic stellate cell activation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM A 191 |
| Chain | Residue |
| A | ALA56 |
| A | HIS117 |
| A | VAL119 |
| A | PHE124 |
| A | CMO192 |
| A | HOH234 |
| A | TYR59 |
| A | PHE60 |
| A | GLN62 |
| A | ARG79 |
| A | HIS81 |
| A | ARG84 |
| A | ALA88 |
| A | HIS113 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CMO A 192 |
| Chain | Residue |
| A | VAL85 |
| A | HEM191 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:15044115, ECO:0000269|PubMed:15095869, ECO:0000269|PubMed:15165856, ECO:0000269|PubMed:16699195, ECO:0007744|PDB:1URV, ECO:0007744|PDB:1URY, ECO:0007744|PDB:1UT0, ECO:0007744|PDB:1UX9, ECO:0007744|PDB:1V5H, ECO:0007744|PDB:2DC3 |
| Chain | Residue | Details |
| A | HIS81 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:15044115, ECO:0000269|PubMed:15095869, ECO:0000269|PubMed:15165856, ECO:0000269|PubMed:16699195, ECO:0007744|PDB:1UMO, ECO:0007744|PDB:1URV, ECO:0007744|PDB:1URY, ECO:0007744|PDB:1UT0, ECO:0007744|PDB:1UX9, ECO:0007744|PDB:1V5H, ECO:0007744|PDB:2DC3 |
| Chain | Residue | Details |
| A | HIS113 |
