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PDBsum entry 4uhh

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protein ligands metals links
Hydrolase PDB id
4uhh

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
273 a.a.
Ligands
CAD
PEG
Metals
_CL
Waters ×458
PDB id:
4uhh
Name: Hydrolase
Title: Structural studies of a thermophilic esterase from thermogutta terrifontis (cacodylate complex)
Structure: Esterase. Chain: a. Engineered: yes
Source: Planctomycetes bacterium r1. Organism_taxid: 1331910. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: arcticexpress ril.
Resolution:
1.06Å     R-factor:   0.104     R-free:   0.123
Authors: C.Sayer,M.N.Isupov,E.Bonch-Osmolovskaya,J.A.Littlechild
Key ref: C.Sayer et al. (2015). Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis. Febs J, 282, 2846-2857. PubMed id: 26011036 DOI: 10.1111/febs.13326
Date:
24-Mar-15     Release date:   10-Jun-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
A0A0H4B872  (A0A0H4B872_9PLAN) -  Alpha/beta hydrolase fold from Thermogutta terrifontis
Seq:
Struc:
274 a.a.
273 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.1.1  - carboxylesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a carboxylic ester + H2O = an alcohol + a carboxylate + H+
carboxylic ester
+ H2O
= alcohol
+ carboxylate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1111/febs.13326 Febs J 282:2846-2857 (2015)
PubMed id: 26011036  
 
 
Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis.
C.Sayer, M.N.Isupov, E.Bonch-Osmolovskaya, J.A.Littlechild.
 
  ABSTRACT  
 
No abstract given.

 

 

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