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 | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 301 |
Chain | Residue |
A | ALA188 |
A | SER260 |
A | PHE261 |
A | HOH426 |
A | HOH548 |
C | PRO9 |
D | LEU25 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 302 |
Chain | Residue |
A | HIS117 |
A | V1F303 |
A | HIS91 |
A | HIS93 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE V1F A 303 |
Chain | Residue |
A | ASN64 |
A | GLN89 |
A | HIS91 |
A | HIS93 |
A | GLU104 |
A | HIS117 |
A | ALA129 |
A | VAL141 |
A | LEU197 |
A | THR198 |
A | THR199 |
A | PRO200 |
A | ZN302 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 301 |
Chain | Residue |
B | ASP156 |
B | SER160 |
B | GLN221 |
B | HOH575 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | ASN152 |
B | SER154 |
B | GLU181 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 303 |
Chain | Residue |
B | HIS91 |
B | HIS93 |
B | HIS117 |
B | V1F304 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE V1F B 304 |
Chain | Residue |
B | ASN64 |
B | GLN89 |
B | HIS91 |
B | HIS93 |
B | HIS117 |
B | VAL119 |
B | ALA129 |
B | SER133 |
B | LEU197 |
B | THR198 |
B | THR199 |
B | PRO200 |
B | PRO201 |
B | TRP208 |
B | ZN303 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 301 |
Chain | Residue |
C | HIS91 |
C | HIS93 |
C | HIS117 |
C | V1F302 |
site_id | AC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE V1F C 302 |
Chain | Residue |
C | ASN64 |
C | GLN89 |
C | HIS91 |
C | HIS93 |
C | HIS117 |
C | VAL119 |
C | ALA129 |
C | SER130 |
C | SER133 |
C | LEU197 |
C | THR198 |
C | THR199 |
C | PRO201 |
C | TRP208 |
C | ZN301 |
C | HOH529 |
C | HOH578 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 301 |
Chain | Residue |
D | HIS91 |
D | HIS93 |
D | HIS117 |
D | V1F302 |
site_id | BC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE V1F D 302 |
Chain | Residue |
D | ASN64 |
D | GLN89 |
D | HIS91 |
D | HIS93 |
D | HIS117 |
D | VAL119 |
D | SER133 |
D | LEU197 |
D | THR198 |
D | THR199 |
D | PRO200 |
D | TRP208 |
D | ZN301 |
D | HOH526 |
D | HOH540 |
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
Chain | Residue | Details |
A | HIS66 | |
B | HIS66 | |
C | HIS66 | |
D | HIS66 | |
Chain | Residue | Details |
A | HIS91 | |
D | HIS91 | |
D | HIS93 | |
D | HIS117 | |
A | HIS93 | |
A | HIS117 | |
B | HIS91 | |
B | HIS93 | |
B | HIS117 | |
C | HIS91 | |
C | HIS93 | |
C | HIS117 | |
Chain | Residue | Details |
A | THR198 | |
B | THR198 | |
C | THR198 | |
D | THR198 | |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN52 | |
A | ASN134 | |
B | ASN52 | |
B | ASN134 | |
C | ASN52 | |
C | ASN134 | |
D | ASN52 | |
D | ASN134 | |