1GTJ
Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Ala-Phe-cho
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 1 | 0004252 | molecular_function | serine-type endopeptidase activity |
| 1 | 0006508 | biological_process | proteolysis |
| 1 | 0008236 | molecular_function | serine-type peptidase activity |
| 2 | 0004252 | molecular_function | serine-type endopeptidase activity |
| 2 | 0006508 | biological_process | proteolysis |
| 2 | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 1 1358 |
| Chain | Residue |
| 1 | SER198 |
| 1 | ALA199 |
| 1 | GLY200 |
| 1 | ARG201 |
| 1 | HOH2197 |
| 1 | HOH2198 |
| 2 | PRO228 |
| 2 | SER229 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA 1 1359 |
| Chain | Residue |
| 1 | ILE317 |
| 1 | GLY334 |
| 1 | GLY336 |
| 1 | ASP338 |
| 1 | HOH2194 |
| 1 | ASP316 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 2 1358 |
| Chain | Residue |
| 1 | PRO228 |
| 1 | SER229 |
| 2 | SER198 |
| 2 | ALA199 |
| 2 | GLY200 |
| 2 | ARG201 |
| 2 | HOH2172 |
| 2 | HOH2173 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA 2 1359 |
| Chain | Residue |
| 2 | ASP316 |
| 2 | ILE317 |
| 2 | GLY334 |
| 2 | GLY336 |
| 2 | ASP338 |
| 2 | HOH2167 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN 3 OF ALDEHYDE INHIBITOR |
| Chain | Residue |
| 1 | GLU78 |
| 1 | ASN102 |
| 1 | SER128 |
| 1 | TRP129 |
| 1 | GLY130 |
| 1 | ASP164 |
| 1 | ASP179 |
| 1 | GLY276 |
| 1 | THR277 |
| 1 | SER278 |
| 1 | HOH2100 |
| 3 | HOH2001 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN 4 OF ALDEHYDE INHIBITOR |
| Chain | Residue |
| 2 | GLU78 |
| 2 | ASN102 |
| 2 | SER128 |
| 2 | TRP129 |
| 2 | GLY130 |
| 2 | ASP164 |
| 2 | ASP179 |
| 2 | GLY276 |
| 2 | THR277 |
| 2 | SER278 |
| 2 | HOH2094 |
| 4 | HOH2001 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"12057200","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15242607","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12057200","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15242607","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GT9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GTG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GTL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T1E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T1I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1nlu |
| Chain | Residue | Details |
| 1 | SER278 | |
| 1 | ASP164 | |
| 1 | ASP82 | |
| 1 | GLU78 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1nlu |
| Chain | Residue | Details |
| 2 | SER278 | |
| 2 | ASP164 | |
| 2 | ASP82 | |
| 2 | GLU78 |






