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PDBsum entry 3tpj
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PDB id:
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Hydrolase
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Title:
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Apo structure of bace1
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Structure:
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Beta-secretase 1. Chain: a. Fragment: unp residues 43-454. Synonym: aspartyl protease 2, asp2, asp 2, beta-site amyloid precursor protein cleaving enzyme 1, beta-site app cleaving enzyme 1, memapsin-2, membrane-associated aspartic protease 2. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: bace, bace1, kiaa1149. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.61Å
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R-factor:
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0.178
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R-free:
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0.196
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Authors:
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Y.C.Xu,M.J.Li,H.Greenblatt,T.T.Chen,I.Silman,J.L.Sussman
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Key ref:
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Y.Xu
et al.
(2012).
Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations.
Acta Crystallogr D Biol Crystallogr,
68,
13-25.
PubMed id:
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Date:
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08-Sep-11
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Release date:
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23-Nov-11
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PROCHECK
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Headers
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References
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P56817
(BACE1_HUMAN) -
Beta-secretase 1 from Homo sapiens
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Seq:
Struc:
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501 a.a.
377 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Acta Crystallogr D Biol Crystallogr
68:13-25
(2012)
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PubMed id:
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Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations.
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Y.Xu,
M.J.Li,
H.Greenblatt,
W.Chen,
A.Paz,
O.Dym,
Y.Peleg,
T.Chen,
X.Shen,
J.He,
H.Jiang,
I.Silman,
J.L.Sussman.
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ABSTRACT
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Links
