Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004089 | molecular_function | carbonate dehydratase activity |
A | 0008270 | molecular_function | zinc ion binding |
B | 0004089 | molecular_function | carbonate dehydratase activity |
B | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | HIS226 |
A | HIS228 |
A | HIS251 |
A | HOH606 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | HIS140 |
A | TRP141 |
A | HIS200 |
B | HIS244 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | HOH506 |
A | HOH638 |
A | HOH755 |
A | GLN224 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | ARG151 |
A | GLN326 |
A | TYR327 |
A | GLU328 |
A | ILE341 |
A | HOH512 |
A | HOH538 |
A | HOH595 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | ARG151 |
A | VAL152 |
A | GLU387 |
A | HOH521 |
A | HOH646 |
B | GLY393 |
B | VAL394 |
B | ASP395 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CL A 406 |
Chain | Residue |
A | ARG159 |
A | GLN338 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CL A 407 |
Chain | Residue |
A | GLU242 |
A | HOH579 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue TRS A 408 |
Chain | Residue |
A | LEU373 |
A | PHE375 |
A | HOH575 |
A | HOH611 |
A | HOH675 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN A 409 |
Chain | Residue |
A | HIS244 |
B | TRP141 |
B | HIS200 |
B | HOH671 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | HIS226 |
B | HIS228 |
B | HIS251 |
B | HOH575 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | GLN224 |
B | VAL253 |
B | HOH586 |
B | HOH602 |
B | HOH611 |
B | HOH683 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | PRO269 |
B | GLY270 |
B | GLU328 |
B | HOH511 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
A | PRO208 |
B | PHE160 |
B | ARG384 |
B | HOH514 |
B | HOH547 |
B | HOH707 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue CL B 405 |
Chain | Residue |
B | ARG159 |
B | GLN338 |
Functional Information from PROSITE/UniProt
site_id | PS00162 |
Number of Residues | 17 |
Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVeghrFpaEIHVV |
Chain | Residue | Details |
A | SER237-VAL253 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS200 | |
B | HIS200 | |
Chain | Residue | Details |
A | HIS226 | |
A | HIS228 | |
A | HIS251 | |
B | HIS226 | |
B | HIS228 | |
B | HIS251 | |
Chain | Residue | Details |
A | THR332 | |
B | THR332 | |
Chain | Residue | Details |
A | ASN346 | |
B | ASN346 | |