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PDBsum entry 5jbt

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protein ligands metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
5jbt

 

 

 

 

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Contents
Protein chains
224 a.a.
14 a.a.
38 a.a.
Ligands
SO4
Metals
_CA
Waters ×261
PDB id:
5jbt
Name: Hydrolase/hydrolase inhibitor
Title: Mesotrypsin in complex with cleaved amyloid precursor like protein 2 inhibitor (aplp2)
Structure: Prss3 protein. Chain: a. Engineered: yes. Mutation: yes. Amyloid-like protein 2. Chain: x. Synonym: aplp-2,apph,amyloid protein homolog,cdei box-binding protein,cdebp. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: pancreas. Gene: prss3. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: aplp2, appl2. Expressed in: komagataella pastoris.
Resolution:
1.40Å     R-factor:   0.165     R-free:   0.199
Authors: O.Kayode,R.Wang,D.Pendlebury,A.Soares,E.S.Radisky
Key ref: O.Kayode et al. (2016). An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis. J Biol Chem, 291, 26304-26319. PubMed id: 27810896 DOI: 10.1074/jbc.M116.758417
Date:
13-Apr-16     Release date:   09-Nov-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P35030  (TRY3_HUMAN) -  Trypsin-3 from Homo sapiens
Seq:
Struc:
304 a.a.
224 a.a.*
Protein chain
Pfam   ArchSchema ?
Q06481  (APLP2_HUMAN) -  Amyloid beta precursor like protein 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
763 a.a.
14 a.a.
Protein chain
Pfam   ArchSchema ?
Q06481  (APLP2_HUMAN) -  Amyloid beta precursor like protein 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
763 a.a.
38 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.4.21.4  - trypsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

 

 
DOI no: 10.1074/jbc.M116.758417 J Biol Chem 291:26304-26319 (2016)
PubMed id: 27810896  
 
 
An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.
O.Kayode, R.Wang, D.F.Pendlebury, I.Cohen, R.D.Henin, A.Hockla, A.S.Soares, N.Papo, T.R.Caulfield, E.S.Radisky.
 
  ABSTRACT  
 
No abstract given.

 

 

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