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 |