2TEC
MOLECULAR DYNAMICS REFINEMENT OF A THERMITASE-EGLIN-C COMPLEX AT 1.98 ANGSTROMS RESOLUTION AND COMPARISON OF TWO CRYSTAL FORMS THAT DIFFER IN CALCIUM CONTENT
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0005576 | cellular_component | extracellular region |
| E | 0006508 | biological_process | proteolysis |
| E | 0008233 | molecular_function | peptidase activity |
| E | 0008236 | molecular_function | serine-type peptidase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0046872 | molecular_function | metal ion binding |
| I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| I | 0009611 | biological_process | response to wounding |
| I | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 343 |
| Chain | Residue |
| E | ASP5 |
| E | ASP47 |
| E | VAL82 |
| E | ASN85 |
| E | THR87 |
| E | ILE89 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 344 |
| Chain | Residue |
| E | THR64 |
| E | GLN66 |
| E | ASP57 |
| E | ASP60 |
| E | ASP62 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 345 |
| Chain | Residue |
| E | ALA173 |
| E | TYR175 |
| E | ALA178 |
| E | ASP201 |
| E | HOH447 |
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 |
| E | ILE34-HIS45 |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThCAGiAAA |
| Chain | Residue | Details |
| E | HIS71-ALA81 |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG |
| Chain | Residue | Details |
| E | GLY223-GLY233 |
| site_id | PS00285 |
| Number of Residues | 12 |
| Details | POTATO_INHIBITOR Potato inhibitor I family signature. FPEVVGktVdqA |
| Chain | Residue | Details |
| I | PHE10-ALA21 |
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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond"} |
| 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 |
| E | ASP38 | |
| E | HIS71 | |
| E | SER225 |
