4HVA
Mechanistic and Structural Understanding of Uncompetitive Inhibitors of Caspase-6
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 4HV B 401 |
| Chain | Residue |
| B | LEU61 |
| D | VAL2 |
| D | GLU3 |
| D | ILE4 |
| D | 4H05 |
| B | HIS121 |
| B | GLY122 |
| B | TYR128 |
| B | HIS168 |
| B | HIS219 |
| B | CYS264 |
| B | LYS265 |
| B | ALA269 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 4HV A 401 |
| Chain | Residue |
| A | LEU61 |
| A | PRO62 |
| A | HIS121 |
| A | GLY122 |
| A | HIS168 |
| A | HIS219 |
| A | CYS264 |
| C | VAL2 |
| C | GLU3 |
| C | ILE4 |
| C | HOH504 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR CHAIN C OF VEID INHIBITOR |
| Chain | Residue |
| A | ARG64 |
| A | ARG65 |
| A | SER120 |
| A | HIS121 |
| A | GLY122 |
| A | GLN161 |
| A | ALA162 |
| A | CYS163 |
| A | TYR217 |
| A | SER218 |
| A | HIS219 |
| A | ARG220 |
| A | THR222 |
| A | PHE263 |
| A | CYS264 |
| A | LYS265 |
| A | 4HV401 |
| A | HOH543 |
| A | HOH610 |
| C | HOH501 |
| C | HOH502 |
| C | HOH503 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR CHAIN D OF VEID INHIBITOR |
| Chain | Residue |
| B | ARG64 |
| B | ARG65 |
| B | SER120 |
| B | HIS121 |
| B | GLY122 |
| B | GLN161 |
| B | CYS163 |
| B | TYR217 |
| B | SER218 |
| B | HIS219 |
| B | ARG220 |
| B | THR222 |
| B | PHE263 |
| B | CYS264 |
| B | LYS265 |
| B | 4HV401 |
| B | HOH522 |
| D | HOH101 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Region: {"description":"Tri-arginine exosite","evidences":[{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Region: {"description":"130's region","evidences":[{"source":"PubMed","id":"28154009","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"16123779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19133298","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19694615","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20890311","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28864531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O08738","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by NUAK1 and AMPK","evidences":[{"source":"PubMed","id":"15273717","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22483120","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32029622","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27911442","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
