1PAU
Crystal structure of the complex of apopain with the tetrapeptide aldehyde inhibitor AC-DEVD-CHO
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 | 15 |
| Details | BINDING SITE FOR CHAIN C OF ACE-ASP-GLU-VAL-ASA |
| Chain | Residue |
| A | SER175 |
| A | ARG179 |
| A | HIS237 |
| A | GLN283 |
| A | CYS285 |
| B | TYR338 |
| B | SER339 |
| B | TRP340 |
| B | ARG341 |
| B | ASN342 |
| B | SER343 |
| B | SER381 |
| B | PHE381 |
| B | HOH626 |
| C | HOH619 |
| site_id | S1 |
| Number of Residues | 10 |
| Details | INHIBITOR BINDING SUB-SITE S1. |
| Chain | Residue |
| A | ARG179 |
| B | ARG341 |
| A | SER236 |
| A | HIS237 |
| A | GLY238 |
| A | GLN283 |
| A | ALA284 |
| A | CYS285 |
| B | SER339 |
| B | TRP340 |
| site_id | S2 |
| Number of Residues | 6 |
| Details | INHIBITOR BINDING SUB-SITE S2. |
| Chain | Residue |
| A | CYS285 |
| B | TYR338 |
| B | SER339 |
| B | TRP340 |
| B | ARG341 |
| B | PHE381 |
| site_id | S3 |
| Number of Residues | 6 |
| Details | INHIBITOR BINDING SUB-SITE S3. |
| Chain | Residue |
| A | SER178 |
| A | ARG179 |
| A | SER180 |
| B | TRP340 |
| B | ARG341 |
| B | SER343 |
| site_id | S4 |
| Number of Residues | 8 |
| Details | INHIBITOR BINDING SUB-SITE S4. |
| Chain | Residue |
| B | TRP340 |
| B | ARG341 |
| B | ASN342 |
| B | GLY346 |
| B | SER347 |
| B | TRP348 |
| B | SER381 |
| B | PHE381 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P29466","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-nitrosocysteine; in inhibited form","evidences":[{"source":"PubMed","id":"10213689","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"(Microbial infection) ADP-riboxanated arginine","evidences":[{"source":"PubMed","id":"35338844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36423631","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qx3 |
| Chain | Residue | Details |
| A | CYS285 | |
| A | HIS237 | |
| A | GLY238 |
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 815 |
| Chain | Residue | Details |
| A | THR177 | electrostatic stabiliser |
| A | SER178 | electrostatic stabiliser |
| A | HIS237 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLY238 | electrostatic stabiliser |
| A | CYS285 | electrostatic stabiliser |
