2QLB
Crystal Structure of caspase-7 with inhibitor AC-ESMD-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 |
| C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008234 | molecular_function | cysteine-type peptidase activity |
| D | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CIT D 850 |
| Chain | Residue |
| A | ARG187 |
| B | PRO227 |
| B | CYS290 |
| C | ARG487 |
| D | TYR523 |
| D | PRO527 |
| D | VAL592 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR CHAIN E OF INHIBITOR AC-ESMD-CHO |
| Chain | Residue |
| A | GLY145 |
| A | GLN184 |
| A | CYS186 |
| B | SER231 |
| B | TRP232 |
| B | ARG233 |
| B | PRO235 |
| B | TRP240 |
| B | SER275 |
| B | GLN276 |
| B | PHE282 |
| B | HOH1105 |
| E | HOH1151 |
| A | ARG87 |
| A | HIS144 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR CHAIN F OF INHIBITOR AC-ESMD-CHO |
| Chain | Residue |
| C | ARG387 |
| C | HIS444 |
| C | GLY445 |
| C | GLN484 |
| C | CYS486 |
| D | TYR530 |
| D | SER531 |
| D | TRP532 |
| D | ARG533 |
| D | PRO535 |
| D | TRP540 |
| D | SER575 |
| D | GLN576 |
| D | PHE582 |
| D | HOH1056 |
| F | HOH1007 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN G OF PEPTIDE QGHGE |
| Chain | Residue |
| A | GLN59 |
| B | LYS254 |
| B | ASP255 |
| B | GLN260 |
| B | TYR300 |
| B | SER302 |
| D | GLN560 |
| D | GLU598 |
| D | TYR600 |
| D | SER602 |
| D | GLN603 |
| D | HOH1117 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Region: {"description":"Loop L1","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Region: {"description":"Loop L2","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11701129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16916640","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in allosteric regulation","evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19581639","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Region: {"description":"Loop L3","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 28 |
| Details | Region: {"description":"Loop L4","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(Microbial infection) ADP-riboxanated arginine","evidences":[{"source":"PubMed","id":"35338844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","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 | CYS186 | |
| A | GLY145 | |
| A | HIS144 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qx3 |
| Chain | Residue | Details |
| C | GLY445 | |
| C | HIS444 | |
| C | CYS486 |
