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2W2M

WT PCSK9-DELTAC BOUND TO WT EGF-A OF LDLR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
E0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA E1334
ChainResidue
ETHR294
EGLU296
EASP310
ELEU311
EGLY314
EHOH2010
EHOH2013

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A1448
ChainResidue
AVAL333
ATHR335
ACYS358
AASP360
AALA328
AALA330

Functional Information from PROSITE/UniProt
site_idPS01187
Number of Residues24
DetailsEGF_CA Calcium-binding EGF-like domain signature. DiDECqdpdt.........Csql....CvNleggYkC
ChainResidueDetails
EASP333-CYS356

site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CnDlkigYeClC
ChainResidueDetails
ECYS308-CYS319
ECYS347-CYS358

site_idPS01186
Number of Residues15
DetailsEGF_2 EGF-like domain signature 2. ClCpdGFqlvaqrr.C
ChainResidueDetails
ECYS317-CYS331
ECYS356-CYS371

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:14622975
ChainResidueDetails
PGLN152
AHIS226
ASER386

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by furin and PCSK5 => ECO:0000269|PubMed:16912035
ChainResidueDetails
AARG218

218853

PDB entries from 2024-04-24

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