4WCX
Crystal structure of HydG: A maturase of the [FeFe]-hydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0042364 | biological_process | water-soluble vitamin biosynthetic process |
| A | 0044272 | biological_process | sulfur compound biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0042364 | biological_process | water-soluble vitamin biosynthetic process |
| C | 0044272 | biological_process | sulfur compound biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 A 501 |
| Chain | Residue |
| A | CYS90 |
| A | ASN92 |
| A | CYS94 |
| A | CYS97 |
| A | LYS210 |
| A | MET503 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 A 502 |
| Chain | Residue |
| A | ASN409 |
| A | ALA505 |
| A | H2S506 |
| A | CYS380 |
| A | CYS383 |
| A | CYS406 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue MET A 503 |
| Chain | Residue |
| A | TYR85 |
| A | TYR99 |
| A | GLU133 |
| A | ALA134 |
| A | ASN169 |
| A | GLN354 |
| A | SF4501 |
| A | HOH955 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue FE A 504 |
| Chain | Residue |
| A | HIS265 |
| A | ALA505 |
| A | H2S506 |
| A | HOH913 |
| A | HOH914 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue ALA A 505 |
| Chain | Residue |
| A | HIS265 |
| A | GLY307 |
| A | SER328 |
| A | GLN329 |
| A | PHE393 |
| A | SF4502 |
| A | FE504 |
| A | H2S506 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue H2S A 506 |
| Chain | Residue |
| A | SF4502 |
| A | FE504 |
| A | ALA505 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue NA A 507 |
| Chain | Residue |
| A | GLU343 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 C 501 |
| Chain | Residue |
| C | CYS90 |
| C | ASN92 |
| C | CYS94 |
| C | CYS97 |
| C | TYR99 |
| C | LYS210 |
| C | SAM503 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 C 502 |
| Chain | Residue |
| C | CYS380 |
| C | CYS383 |
| C | PHE393 |
| C | CYS406 |
| C | ASN409 |
| C | H2S504 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue SAM C 503 |
| Chain | Residue |
| C | TYR96 |
| C | CYS97 |
| C | ALA134 |
| C | ASN169 |
| C | LEU191 |
| C | PHE192 |
| C | GLU194 |
| C | LYS210 |
| C | LEU236 |
| C | ARG271 |
| C | ARG273 |
| C | TYR341 |
| C | HIS342 |
| C | SF4501 |
| C | HOH746 |
| C | HOH929 |
| C | HOH930 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue H2S C 504 |
| Chain | Residue |
| C | VAL79 |
| C | SF4502 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 505 |
| Chain | Residue |
| C | TYR240 |
| C | ARG452 |
| C | ARG456 |
| C | HOH610 |
| C | HOH626 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 506 |
| Chain | Residue |
| C | GLU19 |
| C | LYS22 |
| C | GLU448 |
| C | ARG452 |
| C | HOH622 |
