6CDH
Crystal structure of ferrous form of the Cl-Tyr157 human cysteine dioxygenase with both uncrosslinked and crosslinked cofactor
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 | 0010243 | biological_process | response to organonitrogen compound |
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 | HOH403 |
A | HOH411 |
A | HOH521 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | LYS119 |
A | ARG141 |
A | GLN169 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | GLN34 |
A | ARG123 |
A | ALA131 |
A | TYR132 |
A | HOH408 |
A | HOH421 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 304 |
Chain | Residue |
A | TYR56 |
A | HIS173 |
A | LYS174 |
A | HOH402 |
A | HOH415 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | TYR58 |
A | SER83 |
A | SER84 |
A | HOH406 |
A | HOH409 |
A | HOH506 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL A 306 |
Chain | Residue |
A | SER42 |
A | PRO44 |
A | LEU98 |
A | GLN99 |
A | GLU127 |
A | HOH478 |
A | HOH481 |
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 | 3CT157 |