Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 4uhd
Go to PDB code:
Hydrolase
PDB id
4uhd
Loading ...
Contents
Protein chain
274 a.a.
Ligands
ACT
×2
PEG
×2
Metals
_CL
_MG
Waters
×366
PDB id:
4uhd
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Hydrolase
Title:
Structural studies of a thermophilic esterase from thermogutta terrifontis (acetate bound)
Structure:
Esterase. Chain: a. Engineered: yes
Source:
Planctomycetes bacterium r1. Organism_taxid: 1331910. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.07Å
R-factor:
0.094
R-free:
0.112
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
Headers
References
Protein chain
?
A0A0M3KKY6
(A0A0M3KKY6_9BACT) - Esterase from Thermogutta terrifontis
Seq:
Struc:
282 a.a.
274 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
Bound ligand (Het Group name =
ACT
)
matches with 60.00% similarity
+
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.
'); } }