7ANQ: Complete PCSK9 C-ter domain

Complete PCSK9 C-ter domain in complex with VHH P1.40. Determined by X-ray diffraction at 2.2 Å resolution. Released 20 Oct 2021.

Method: X-ray diffraction
Resolution: 2.2 Å
Organisms: Homo sapiens, Lama glama
Chains: 2
Atoms: 2,819
Mol. weight: 39.52 kDa
Released: 20 Oct 2021

Explore 7ANQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7ANQ contains 8 α-helices and 30 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	456-461	6	1
α-helix	462-464	3
β-strand	472-475	4	2
β-strand	482-489	8	1
β-strand	495-496	2	2
β-strand	497	1	3
β-strand	498-503	6	2
β-strand	506-513	8	2
α-helix	514	1
β-strand	521-528	8	1
β-strand	533-539	7	3
β-strand	548-551	4	4
β-strand	558-566	9	3
β-strand	587-590	4	4
β-strand	594-602	9	3
β-strand	606-615	10	5
β-strand	621-625	5	1
α-helix	626-627	2
β-strand	631-637	7	5
α-helix	638	1
β-strand	644-650	7	1
β-strand	653-658	6	1
α-helix	661-663	3
β-strand	672-681	10	5

Chain B: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	6
β-strand	10-13	4	7
β-strand	18-24	7	6
β-strand	33-39	7	7
β-strand	46-51	6	7
β-strand	59-60	2	7
α-helix	62-64	3
β-strand	68-73	6	6
β-strand	78-83	6	6
α-helix	88-90	3
β-strand	92-99	8	7
α-helix	111-113	3
β-strand	116-117	2	7
β-strand	121-126	6	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Proprotein convertase subtilisin/kexin type 9	A	protein	231	Homo sapiens	Q8NBP7 (AlphaFold model)
VHH P1.40 minibody anti-Cter PCSK9	B	protein	127	Lama glama

Sequence of entity 1 (A), FASTA

>7ANQ_1 Proprotein convertase subtilisin/kexin type 9 (chains A)
GWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRA
HNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHWEVEDL
GTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWT
LTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRSR

Sequence of entity 2 (B), FASTA

>7ANQ_2 VHH P1.40 minibody anti-Cter PCSK9 (chains B)
QVKLEESGGGLVQAGGSLRLSCSPSDRTFSAYAMGWFRQVPGREREFVATIRDSDASIYY
TDSVKGRFTISRDNAKNTVYLQMNSLIPDDTAVYYCAARQYYSGRVYSTFREEYDYWGQG
TQVTVSS

Primary citation

Molecular interactions of PCSK9 with an inhibitory nanobody, CAP1 and HLA-C: Functional regulation of LDLR levels. Fruchart Gaillard, C., Ouadda, A.B.D., Ciccone, L. et al. Mol Metab (2022) 67:101662-101662. DOI 10.1016/j.molmet.2022.101662 · PubMed

Other PDB entries of the same protein (UniProt Q8NBP7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7S5H 1.27 Å, PCSK9(deltaCRD) in complex with cyclic peptide 35
6XIC 1.38 Å, PCSK9(deltaCRD) in complex with cyclic peptide 40
6XIE 1.43 Å, PCSK9(deltaCRD) in complex with cyclic peptide 77
9HZ3 1.43 Å, PCSK9 AZD0780 complex
6XID 1.48 Å, PCSK9(deltaCRD) in complex with cyclic peptide 51
6U26 1.53 Å, PCSK9 in complex with compound 16
6XIB 1.55 Å, PCSK9(deltaCRD) in complex with cyclic peptide 30
9SZY 1.76 Å, PCSK9 CTD fragment structure
6XIF 1.77 Å, PCSK9(deltaCRD) in complex with cyclic peptide 83
10SB 1.83 Å, PCSK9 in complex with cyclic peptide 21
4NMX 1.85 Å, PCSK9(deltaCRD) in complex with phage-derived inhibitory peptide 2-8
2QTW 1.9 Å, The Crystal Structure of PCSK9 at 1.9 Angstroms Resolution Reveals structural homology…

Browse structure collections

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