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 |
C | 0004089 | molecular_function | carbonate dehydratase activity |
C | 0008270 | molecular_function | zinc ion binding |
D | 0004089 | molecular_function | carbonate dehydratase activity |
D | 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 301 |
Chain | Residue |
A | HIS91 |
A | HIS93 |
A | HIS117 |
A | VD8302 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue VD8 A 302 |
Chain | Residue |
A | LEU197 |
A | THR198 |
A | THR199 |
A | ZN301 |
A | ASN64 |
A | GLN89 |
A | HIS91 |
A | HIS93 |
A | HIS117 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | HIS91 |
B | HIS93 |
B | HIS117 |
B | VD8302 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue VD8 B 302 |
Chain | Residue |
B | ASN64 |
B | GLN89 |
B | HIS91 |
B | HIS93 |
B | HIS117 |
B | LEU197 |
B | THR198 |
B | THR199 |
B | ZN301 |
B | HOH464 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | THR44 |
B | GLY80 |
B | LEU81 |
B | TYR190 |
B | ARG192 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN C 301 |
Chain | Residue |
C | HIS91 |
C | HIS93 |
C | HIS117 |
C | VD8302 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue VD8 C 302 |
Chain | Residue |
C | ASN64 |
C | GLN89 |
C | HIS91 |
C | HIS93 |
C | HIS117 |
C | VAL119 |
C | LEU197 |
C | THR198 |
C | THR199 |
C | ZN301 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
C | TRP4 |
C | TYR19 |
C | HOH477 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue EDO C 304 |
Chain | Residue |
C | SER42 |
C | THR44 |
C | LEU46 |
C | GLY80 |
C | TYR190 |
C | ARG192 |
C | HOH432 |
C | HOH447 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO C 305 |
Chain | Residue |
C | LYS166 |
C | THR227 |
C | ALA228 |
C | TYR230 |
C | GLU241 |
C | HOH498 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue ZN D 301 |
Chain | Residue |
D | HIS91 |
D | HIS93 |
D | HIS117 |
D | VD8302 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residue VD8 D 302 |
Chain | Residue |
D | ASN64 |
D | GLN89 |
D | HIS91 |
D | HIS93 |
D | HIS117 |
D | LEU197 |
D | THR198 |
D | THR199 |
D | ZN301 |
D | HOH441 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
D | THR44 |
D | LEU46 |
D | GLY80 |
D | TYR190 |
D | ARG192 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
D | ASP156 |
D | SER160 |
Functional Information from PROSITE/UniProt
site_id | PS00162 |
Number of Residues | 17 |
Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVsgqhFaaELHIV |
Chain | Residue | Details |
A | SER103-VAL119 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"11493685","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |