3S67
Crystal structure of V57P mutant of human cystatin C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001540 | molecular_function | amyloid-beta binding |
| A | 0002020 | molecular_function | protease binding |
| A | 0004866 | molecular_function | endopeptidase inhibitor activity |
| A | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006952 | biological_process | defense response |
| A | 0006955 | biological_process | immune response |
| A | 0010711 | biological_process | negative regulation of collagen catabolic process |
| A | 0010716 | biological_process | negative regulation of extracellular matrix disassembly |
| A | 0030414 | molecular_function | peptidase inhibitor activity |
| A | 0031982 | cellular_component | vesicle |
| A | 0034103 | biological_process | regulation of tissue remodeling |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045861 | biological_process | negative regulation of proteolysis |
| A | 0060311 | biological_process | negative regulation of elastin catabolic process |
| A | 0060313 | biological_process | negative regulation of blood vessel remodeling |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097435 | biological_process | supramolecular fiber organization |
| A | 1904724 | cellular_component | tertiary granule lumen |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 121 |
| Chain | Residue |
| A | ARG51 |
| A | ARG53 |
| A | PEG123 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 122 |
| Chain | Residue |
| A | ARG25 |
| A | VAL104 |
| A | GLY108 |
| A | THR109 |
| A | MET110 |
| A | HOH180 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 123 |
| Chain | Residue |
| A | TYR42 |
| A | ARG51 |
| A | LEU91 |
| A | PEG121 |
| A | HOH191 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD A 125 |
| Chain | Residue |
| A | HOH182 |
| A | HOH182 |
| A | HOH184 |
| A | HOH184 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT A 127 |
| Chain | Residue |
| A | HOH175 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 128 |
| Chain | Residue |
| A | LYS54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Secondary area of contact"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive site"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
