3T52

L29I Mutation in an Aryl Esterase from Pseudomonas fluorescens Leads to Unique Peptide Flip and Increased Activity


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.211 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.185 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

L29I Mutation in an Aryl Esterase from Pseudomonas fluorescens Leads to Unique Peptide Flip and Increased Activity

Yin, T.Kazlauskas, R.J.Purpero, V.M.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Arylesterase
A, B, C, D, E
A, B, C, D, E, F
271Pseudomonas fluorescensMutation(s): 1 
EC: 3.1.1.2 (PDB Primary Data), 1 (PDB Primary Data)
UniProt
Find proteins for P22862 (Pseudomonas fluorescens)
Explore P22862 
Go to UniProtKB:  P22862
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22862
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

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EB [auth D]
H [auth A]
LC [auth F]
MA [auth C]
MC [auth F]
EB [auth D],
H [auth A],
LC [auth F],
MA [auth C],
MC [auth F],
NA [auth C],
NC [auth F],
OA [auth C],
TB [auth E],
U [auth B],
UB [auth E],
V [auth B]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
GOL
Query on GOL

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AB [auth C]
AC [auth E]
BB [auth C]
CB [auth D]
DB [auth D]
AB [auth C],
AC [auth E],
BB [auth C],
CB [auth D],
DB [auth D],
G [auth A],
HB [auth D],
IA [auth B],
IC [auth E],
JA [auth B],
KA [auth C],
KB [auth D],
KC [auth F],
LA [auth C],
M [auth A],
OB [auth D],
OC [auth F],
PB [auth D],
QB [auth D],
R [auth A],
RA [auth C],
RB [auth E],
S [auth B],
SB [auth E],
SC [auth F],
T [auth B],
WB [auth E],
WC [auth F],
X [auth B],
XC [auth F],
Y [auth B],
ZC [auth F]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
ACT
Query on ACT

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CC [auth E]
DA [auth B]
DC [auth E]
EA [auth B]
EC [auth E]
CC [auth E],
DA [auth B],
DC [auth E],
EA [auth B],
EC [auth E],
FA [auth B],
FC [auth E],
GA [auth B],
GB [auth D],
GC [auth E],
HA [auth B],
JC [auth E],
MB [auth D],
N [auth A],
NB [auth D],
O [auth A],
P [auth A],
Q [auth A],
TA [auth C],
TC [auth F],
UA [auth C],
UC [auth F],
VA [auth C],
VC [auth F],
XA [auth C],
YA [auth C],
YC [auth F],
ZA [auth C]
ACETATE ION
C2 H3 O2
QTBSBXVTEAMEQO-UHFFFAOYSA-M
CL
Query on CL

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FB [auth D]
I [auth A]
J [auth A]
PA [auth C]
QA [auth C]
FB [auth D],
I [auth A],
J [auth A],
PA [auth C],
QA [auth C],
VB [auth E],
W [auth B]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
PEO
Query on PEO

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AA [auth B]
BA [auth B]
BC [auth E]
CA [auth B]
HC [auth E]
AA [auth B],
BA [auth B],
BC [auth E],
CA [auth B],
HC [auth E],
IB [auth D],
JB [auth D],
K [auth A],
L [auth A],
LB [auth D],
PC [auth F],
QC [auth F],
RC [auth F],
SA [auth C],
WA [auth C],
XB [auth E],
YB [auth E],
Z [auth B],
ZB [auth E]
HYDROGEN PEROXIDE
H2 O2
MHAJPDPJQMAIIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.211 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.185 
  • Space Group: P 32
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 146.02α = 90
b = 146.02β = 90
c = 128.95γ = 120
Software Package:
Software NamePurpose
d*TREKdata scaling
d*TREKdata reduction
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-08-01
    Type: Initial release
  • Version 1.1: 2024-02-28
    Changes: Data collection, Database references, Derived calculations