1THM
CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 301 |
| Chain | Residue |
| A | ASP5 |
| A | ASP47 |
| A | VAL82 |
| A | ASN85 |
| A | THR87 |
| A | ILE89 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 302 |
| Chain | Residue |
| A | ASP57 |
| A | ASP62 |
| A | THR64 |
| A | GLN66 |
| A | HOH353 |
| A | HOH370 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 303 |
| Chain | Residue |
| A | ALA173 |
| A | TYR175 |
| A | ALA178 |
| A | ASP201 |
| A | HOH335 |
| A | HOH420 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | SER191 |
| A | SER192 |
| A | PHE193 |
| A | SER207 |
| A | HOH416 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 305 |
| Chain | Residue |
| A | GLN144 |
| A | TYR175 |
| A | SER176 |
| A | HOH320 |
| A | HOH350 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 306 |
| Chain | Residue |
| A | PHE8 |
| A | SER9 |
| A | GLN16 |
| A | ASN140 |
| A | SER141 |
| A | HOH455 |
| site_id | ACT |
| Number of Residues | 3 |
| Details | ENZYME CATALYTIC SITE |
| Chain | Residue |
| A | ASP38 |
| A | HIS71 |
| A | SER225 |
| site_id | IO1 |
| Number of Residues | 6 |
| Details | ION BINDING SITE 1 |
| Chain | Residue |
| A | ASP5 |
| A | ASP47 |
| A | VAL82 |
| A | ASN85 |
| A | THR87 |
| A | ILE89 |
| site_id | IO2 |
| Number of Residues | 6 |
| Details | ION BINDING SITE 2 |
| Chain | Residue |
| A | ASP57 |
| A | ASP62 |
| A | THR64 |
| A | GLN66 |
| A | HOH353 |
| A | HOH370 |
| site_id | IO3 |
| Number of Residues | 6 |
| Details | ION BINDING SITE 3 |
| Chain | Residue |
| A | ALA173 |
| A | TYR175 |
| A | ALA178 |
| A | ASP201 |
| A | HOH335 |
| A | HOH420 |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. IAIVDTGVqsnH |
| Chain | Residue | Details |
| A | ILE34-HIS45 |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThCAGiAAA |
| Chain | Residue | Details |
| A | HIS71-ALA81 |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG |
| Chain | Residue | Details |
| A | GLY223-GLY233 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 265 |
| Details | Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1993669","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2688688","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TEC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TEC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"2688688","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TEC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1993669","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TEC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| A | ASP38 | |
| A | HIS71 | |
| A | SER225 |
