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 |