5OPQ
A 3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides.
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue MPD A 701 |
| Chain | Residue |
| A | ASN218 |
| A | GLY219 |
| A | LEU536 |
| A | GLN566 |
| A | MPD702 |
| A | TRS703 |
| A | HOH827 |
| A | HOH963 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue MPD A 702 |
| Chain | Residue |
| A | GLU537 |
| A | ASP538 |
| A | MPD701 |
| A | HOH889 |
| A | HOH963 |
| A | HOH1034 |
| A | HOH1089 |
| B | HOH842 |
| B | HOH1084 |
| B | HOH1379 |
| A | LEU536 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue TRS A 703 |
| Chain | Residue |
| A | HIS347 |
| A | ASP486 |
| A | ILE487 |
| A | GLU517 |
| A | LYS564 |
| A | ILE565 |
| A | GLN566 |
| A | MPD701 |
| A | HOH911 |
| A | HOH1100 |
| B | CYS198 |
| B | ASP202 |
| B | HOH869 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 704 |
| Chain | Residue |
| A | ARG590 |
| A | HOH1256 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue MPD B 701 |
| Chain | Residue |
| A | LYS208 |
| B | GLU537 |
| B | ASP538 |
| B | HOH844 |
| B | HOH893 |
| B | HOH990 |
| B | HOH1334 |
| B | HOH1393 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue TRS B 702 |
| Chain | Residue |
| A | CYS198 |
| A | ASP202 |
| A | HOH813 |
| B | HIS347 |
| B | TRP455 |
| B | ASP486 |
| B | ILE487 |
| B | GLU517 |
| B | LYS564 |
| B | GLN566 |
| B | HOH856 |
| B | HOH1032 |
| B | HOH1160 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 703 |
| Chain | Residue |
| B | ARG590 |
| B | HOH1267 |
| B | HOH1282 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue MPD C 701 |
| Chain | Residue |
| C | ASN218 |
| C | GLY219 |
| C | LEU536 |
| C | GLN566 |
| C | TRS703 |
| C | HOH920 |
| C | HOH957 |
| C | HOH1082 |
| C | HOH1402 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue TRS C 702 |
| Chain | Residue |
| C | HIS347 |
| C | TRP455 |
| C | ASP486 |
| C | ILE487 |
| C | GLU517 |
| C | LYS564 |
| C | GLN566 |
| C | HOH891 |
| C | HOH1091 |
| D | CYS198 |
| D | ASP202 |
| D | HOH848 |
| site_id | AD1 |
| Number of Residues | 11 |
| Details | binding site for residue TRS C 703 |
| Chain | Residue |
| C | GLU537 |
| C | ASP538 |
| C | MPD701 |
| C | HOH814 |
| C | HOH818 |
| C | HOH957 |
| C | HOH986 |
| C | HOH988 |
| C | HOH1082 |
| D | LYS208 |
| D | HOH821 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 704 |
| Chain | Residue |
| C | ARG590 |
| C | HOH1292 |
| C | HOH1330 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue MPD D 701 |
| Chain | Residue |
| D | HOH805 |
| D | HOH882 |
| D | HOH979 |
| C | HOH902 |
| C | HOH1364 |
| C | HOH1420 |
| D | LEU536 |
| D | GLU537 |
| D | ASP538 |
| site_id | AD4 |
| Number of Residues | 15 |
| Details | binding site for residue TRS D 702 |
| Chain | Residue |
| C | CYS198 |
| C | ASP202 |
| C | HOH848 |
| D | PRO346 |
| D | HIS347 |
| D | TYR422 |
| D | TRP455 |
| D | ASP486 |
| D | ILE487 |
| D | GLU517 |
| D | LYS564 |
| D | ILE565 |
| D | GLN566 |
| D | HOH816 |
| D | HOH1130 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 703 |
| Chain | Residue |
| D | ARG590 |
| D | HOH1221 |
| D | HOH1282 |
