3DAF
The crystal structure of [Fe]-hydrogenase holoenzyme (HMD) from METHANOCALDOCOCCUS JANNASCHII cocrystallized with cyanide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0015948 | biological_process | methanogenesis |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019386 | biological_process | methanogenesis, from carbon dioxide |
A | 0047068 | molecular_function | N5,N10-methenyltetrahydromethanopterin hydrogenase activity |
A | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FEG A 501 |
Chain | Residue |
A | LEU6 |
A | PRO65 |
A | PRO114 |
A | PRO115 |
A | CYS118 |
A | ASP135 |
A | TRP148 |
A | LEU149 |
A | PRO150 |
A | ILE158 |
A | ALA175 |
A | GLY7 |
A | CYS176 |
A | THR177 |
A | PRO202 |
A | CYS204 |
A | PRO206 |
A | HOH2053 |
A | HOH2067 |
A | HOH2068 |
A | ALA8 |
A | GLY9 |
A | CYS10 |
A | THR13 |
A | HIS14 |
A | SER63 |
A | ASP64 |