5OCR
Crystal structure of the kappa-carrageenase zobellia_236 from Zobellia galactanivorans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | SER139 |
| A | TRP141 |
| A | GLU159 |
| A | GLU164 |
| A | ARG263 |
| A | HOH542 |
| A | HOH597 |
| A | HOH635 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | GLY87 |
| A | ASP299 |
| A | HOH511 |
| A | HOH561 |
| A | GLU51 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | PHE52 |
| A | ASN53 |
| A | ASN55 |
| A | ILE84 |
| A | SER85 |
| A | ASN86 |
| A | GLY87 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | SER139 |
| B | TRP141 |
| B | GLU159 |
| B | GLU164 |
| B | ARG263 |
| B | HOH541 |
| B | HOH619 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | GLU51 |
| B | GLY87 |
| B | ASP299 |
| B | HOH586 |
| B | HOH610 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | PHE52 |
| B | ASN53 |
| B | LYS54 |
| B | ASN55 |
| B | ILE84 |
| B | ASN86 |
| B | GLY87 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| B | TYR203 |
| B | PRO204 |
| B | GLN205 |
| B | GLU206 |
| D | ASN152 |
| D | LYS190 |
| D | GLU191 |
| D | ASN192 |
| D | GLY193 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 401 |
| Chain | Residue |
| C | SER139 |
| C | GLU159 |
| C | GLU164 |
| C | ARG263 |
| C | HOH527 |
| C | HOH624 |
| C | HOH633 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 402 |
| Chain | Residue |
| A | LYS190 |
| A | GLY193 |
| C | TYR203 |
| C | PRO204 |
| C | GLN205 |
| C | GLU206 |
| C | HOH543 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 403 |
| Chain | Residue |
| A | HOH523 |
| C | GLU51 |
| C | GLY87 |
| C | ASP299 |
| C | HOH608 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 404 |
| Chain | Residue |
| A | HOH565 |
| C | PHE52 |
| C | ASN53 |
| C | ASN55 |
| C | ILE84 |
| C | ASN86 |
| C | GLY87 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 401 |
| Chain | Residue |
| D | SER139 |
| D | TRP141 |
| D | GLU159 |
| D | GLU164 |
| D | ARG263 |
| D | HOH549 |
| D | HOH627 |
| D | HOH652 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 402 |
| Chain | Residue |
| B | HOH548 |
| D | GLU51 |
| D | GLY87 |
| D | ASP299 |
| D | HOH589 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue MG D 403 |
| Chain | Residue |
| B | HOH600 |
| D | PHE52 |
| D | ASN55 |
| D | ILE84 |
| D | SER85 |
| D | ASN86 |
| D | GLY87 |
