6BGM
Crystal structure of ferrous form of the crosslinked human cysteine dioxygenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000097 | biological_process | sulfur amino acid biosynthetic process |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006534 | biological_process | cysteine metabolic process |
| A | 0006954 | biological_process | inflammatory response |
| A | 0007595 | biological_process | lactation |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0017172 | molecular_function | cysteine dioxygenase activity |
| A | 0019448 | biological_process | L-cysteine catabolic process |
| A | 0033762 | biological_process | response to glucagon |
| A | 0042412 | biological_process | taurine biosynthetic process |
| A | 0043200 | biological_process | response to amino acid |
| A | 0045471 | biological_process | response to ethanol |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0051384 | biological_process | response to glucocorticoid |
| A | 0051591 | biological_process | response to cAMP |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue FE2 A 301 |
| Chain | Residue |
| A | HIS86 |
| A | HIS88 |
| A | HIS140 |
| A | HOH408 |
| A | HOH415 |
| A | HOH464 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | TYR132 |
| A | HOH401 |
| A | HOH429 |
| A | HOH431 |
| A | GLN34 |
| A | ARG123 |
| A | ALA131 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | LYS119 |
| A | ARG141 |
| A | GLN169 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 304 |
| Chain | Residue |
| A | TYR56 |
| A | HIS173 |
| A | LYS174 |
| A | HOH419 |
| A | HOH420 |
| A | HOH454 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 305 |
| Chain | Residue |
| A | ALA166 |
| A | ASP168 |
| A | ASN175 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | ARG10 |
| A | ASP14 |
| A | LYS52 |
| A | GLY186 |
| A | ARG188 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17135237 |
| Chain | Residue | Details |
| A | HIS86 | |
| A | HIS88 | |
| A | HIS140 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | CROSSLNK: 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) => ECO:0000269|PubMed:17135237 |
| Chain | Residue | Details |
| A | CYS93 | |
| A | TYR157 |
