2A5V
Crystal structure of M. tuberculosis beta carbonic anhydrase, Rv3588c, tetrameric form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0005515 | molecular_function | protein binding |
| 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 |
| C | 0004089 | molecular_function | carbonate dehydratase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0015976 | biological_process | carbon utilization |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004089 | molecular_function | carbonate dehydratase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0015976 | biological_process | carbon utilization |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SCN A 501 |
| Chain | Residue |
| A | CYS51 |
| A | ASP53 |
| A | HIS104 |
| A | CYS107 |
| A | GLY108 |
| A | ZN401 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | SCN501 |
| A | CYS51 |
| A | HIS104 |
| A | CYS107 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 405 |
| Chain | Residue |
| A | HIS-3 |
| A | HIS0 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 409 |
| Chain | Residue |
| A | HIS158 |
| A | ASP198 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 400 |
| Chain | Residue |
| A | HIS-4 |
| A | HIS-2 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SCN B 502 |
| Chain | Residue |
| A | TYR89 |
| B | ASP53 |
| B | HIS104 |
| B | CYS107 |
| B | GLY108 |
| B | ZN402 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | CYS51 |
| B | HIS104 |
| B | CYS107 |
| B | SCN502 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B 408 |
| Chain | Residue |
| B | HIS-2 |
| B | HIS0 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SCN C 503 |
| Chain | Residue |
| C | CYS51 |
| C | ASP53 |
| C | HIS104 |
| C | CYS107 |
| C | GLY108 |
| C | ZN403 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SCN C 504 |
| Chain | Residue |
| C | GLN42 |
| D | ASP53 |
| D | ALA75 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 403 |
| Chain | Residue |
| C | CYS51 |
| C | HIS104 |
| C | CYS107 |
| C | SCN503 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 404 |
| Chain | Residue |
| D | CYS51 |
| D | HIS104 |
| D | CYS107 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN D 406 |
| Chain | Residue |
| D | HIS-3 |
| D | HIS-1 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN D 407 |
| Chain | Residue |
| D | HIS-2 |
| D | HIS0 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN D 410 |
| Chain | Residue |
| D | HIS158 |
| D | ASP198 |
Functional Information from PROSITE/UniProt
| site_id | PS00704 |
| Number of Residues | 8 |
| Details | PROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CADSRVaA |
| Chain | Residue | Details |
| A | CYS51-ALA58 |
| site_id | PS00705 |
| Number of Residues | 21 |
| Details | PROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. EYAVtvLnvplIVVlGHdsCG |
| Chain | Residue | Details |
| A | GLU88-GLY108 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15753099","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16321983","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A5V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15753099","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YM3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| A | ASP53 | |
| A | ARG55 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| B | ASP53 | |
| B | ARG55 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| C | ASP53 | |
| C | ARG55 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| D | ASP53 | |
| D | ARG55 |
