Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4OV6

Crystal structure of PCSK9(53-451) with Adnectin

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
E0004252molecular_functionserine-type endopeptidase activity
E0006508biological_processproteolysis
E0008236molecular_functionserine-type peptidase activity
F0005178molecular_functionintegrin binding
F0005201molecular_functionextracellular matrix structural constituent
F0007044biological_processcell-substrate junction assembly
F0007160biological_processcell-matrix adhesion
F0007399biological_processnervous system development
F0007507biological_processheart development
F0043394molecular_functionproteoglycan binding
G0005178molecular_functionintegrin binding
G0005201molecular_functionextracellular matrix structural constituent
G0007044biological_processcell-substrate junction assembly
G0007160biological_processcell-matrix adhesion
G0007399biological_processnervous system development
G0007507biological_processheart development
G0043394molecular_functionproteoglycan binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 201
ChainResidue
ATRP72
APHE150
BLYS258
FHIS80

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 501
ChainResidue
BPHE318
BARG319

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
BPHE379

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 B 503
ChainResidue
EGLN413
BGLN413
BILE416

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 D 201
ChainResidue
DLEU108
DLYS125
DMET126
DHOH308

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP
ChainResidueDetails
FGLY37-PRO44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
BASP186
BHIS226
BSER386
EASP186
EHIS226
ESER386

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by furin and PCSK5 => ECO:0000269|PubMed:16912035
ChainResidueDetails
BARG218
EARG218

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon