4WAJ
H. influenzae beta-carbonic anhydase variant P48S/A49P
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015976 | biological_process | carbon utilization |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015976 | biological_process | carbon utilization |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal 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 | CYS42 |
| A | ASP44 |
| A | HIS98 |
| A | CYS101 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | ARG160 |
| A | LYS165 |
| A | ARG198 |
| B | ARG124 |
| B | PHE128 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | GLY192 |
| A | SER204 |
| B | GLN191 |
| B | GLY192 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | CYS42 |
| B | ASP44 |
| B | HIS98 |
| B | CYS101 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| A | ASP110 |
| A | ARG124 |
| B | ARG160 |
| B | LYS165 |
| B | ARG198 |
| B | HOH440 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| A | SER48 |
| A | PRO49 |
| A | GLU50 |
| A | ARG64 |
| B | SER48 |
| B | PRO49 |
| B | GLU50 |
| B | ARG64 |
Functional Information from PROSITE/UniProt
| site_id | PS00704 |
| Number of Residues | 8 |
| Details | PROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CSDSRVsP |
| Chain | Residue | Details |
| A | CYS42-PRO49 |
| site_id | PS00705 |
| Number of Residues | 21 |
| Details | PROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QYAVdvLkiehIIIcGHtnCG |
| Chain | Residue | Details |
| A | GLN82-GLY102 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16584170","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A8D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
