4OV6
Crystal structure of PCSK9(53-451) with Adnectin
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008236 | molecular_function | serine-type peptidase activity |
E | 0004252 | molecular_function | serine-type endopeptidase activity |
E | 0006508 | biological_process | proteolysis |
E | 0008236 | molecular_function | serine-type peptidase activity |
F | 0005178 | molecular_function | integrin binding |
F | 0005201 | molecular_function | extracellular matrix structural constituent |
F | 0007044 | biological_process | cell-substrate junction assembly |
F | 0007160 | biological_process | cell-matrix adhesion |
F | 0007399 | biological_process | nervous system development |
F | 0007507 | biological_process | heart development |
F | 0043394 | molecular_function | proteoglycan binding |
G | 0005178 | molecular_function | integrin binding |
G | 0005201 | molecular_function | extracellular matrix structural constituent |
G | 0007044 | biological_process | cell-substrate junction assembly |
G | 0007160 | biological_process | cell-matrix adhesion |
G | 0007399 | biological_process | nervous system development |
G | 0007507 | biological_process | heart development |
G | 0043394 | molecular_function | proteoglycan binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 201 |
Chain | Residue |
A | TRP72 |
A | PHE150 |
B | LYS258 |
F | HIS80 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 501 |
Chain | Residue |
B | PHE318 |
B | ARG319 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO B 502 |
Chain | Residue |
B | PHE379 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 B 503 |
Chain | Residue |
E | GLN413 |
B | GLN413 |
B | ILE416 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 D 201 |
Chain | Residue |
D | LEU108 |
D | LYS125 |
D | MET126 |
D | HOH308 |
Functional Information from PROSITE/UniProt
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP |
Chain | Residue | Details |
F | GLY37-PRO44 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 |
Chain | Residue | Details |
B | ASP186 | |
B | HIS226 | |
B | SER386 | |
E | ASP186 | |
E | HIS226 | |
E | SER386 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by furin and PCSK5 => ECO:0000269|PubMed:16912035 |
Chain | Residue | Details |
B | ARG218 | |
E | ARG218 |