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PDBsum entry 3nzi

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protein ligands links
Hydrolase/hydrolase substrate PDB id
3nzi

 

 

 

 

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Contents
Protein chain
211 a.a. *
Ligands
MET-PHE-LYS-LEU-
B2V
* Residue conservation analysis
PDB id:
3nzi
Name: Hydrolase/hydrolase substrate
Title: Substrate induced remodeling of the active site regulates htra1 activity
Structure: Serine protease htra1. Chain: a. Fragment: unp residues 158-480. Synonym: l56, serine protease 11. Engineered: yes. Citrate synthase. Chain: b. Fragment: unp residues 371-377. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: htra1, htra, prss11. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: peptidyl boronic acid inhibitor
Resolution:
2.75Å     R-factor:   0.202     R-free:   0.249
Authors: L.Truebestein,A.Tennstaedt,P.Hauske,T.Krojer,M.Kaiser,T.Clausen, M.Ehrmann
Key ref: L.Truebestein et al. (2011). Substrate-induced remodeling of the active site regulates human HTRA1 activity. Nat Struct Biol, 18, 386-388. PubMed id: 21297635
Date:
16-Jul-10     Release date:   23-Feb-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q92743  (HTRA1_HUMAN) -  Serine protease HTRA1 from Homo sapiens
Seq:
Struc:
480 a.a.
211 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Nat Struct Biol 18:386-388 (2011)
PubMed id: 21297635  
 
 
Substrate-induced remodeling of the active site regulates human HTRA1 activity.
L.Truebestein, A.Tennstaedt, T.Mönig, T.Krojer, F.Canellas, M.Kaiser, T.Clausen, M.Ehrmann.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22245966 H.Malet, F.Canellas, J.Sawa, J.Yan, K.Thalassinos, M.Ehrmann, T.Clausen, and H.R.Saibil (2012).
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.
  Nat Struct Mol Biol, 19, 152-157.
PDB codes: 4a8a 4a8b 4a8c 4a8d 4a9g
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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