3E0X

The crystal structure of a Lipase-esterase related protein from Clostridium acetobutylicum ATCC 824

PDB DOI: https://doi.org/10.2210/pdb3E0X/pdb

Classification: structural genomics, unknown function
Organism(s): Clostridium acetobutylicum
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2008-08-01 Released: 2008-09-30
Deposition Author(s): Tan, K., Sather, A., Cobb, G., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.45 Å
R-Value Free: 0.185
R-Value Work: 0.143
R-Value Observed: 0.145

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

The crystal structure of a Lipase-esterase related protein from Clostridium acetobutylicum ATCC 824

Tan, K., Sather, A., Cobb, G., Joachimiak, A.

To be published.

Macromolecule Content

Total Structure Weight: 55.47 kDa
Atom Count: 4,771
Modelled Residue Count: 488
Deposited Residue Count: 490
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Lipase-esterase related protein	A, B	245	Clostridium acetobutylicum	Mutation(s): 0 Gene Names: CA_C0816
UniProt
Find proteins for Q97KV0 (Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)) Explore Q97KV0 Go to UniProtKB: Q97KV0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q97KV0
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
OXE Query on OXE Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B]	C [auth A], D [auth B]	ORTHO-XYLENE C₈ H₁₀ CTQNGGLPUBDAKN-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Focus chain D [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth B]

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.45 Å
R-Value Free: 0.185
R-Value Work: 0.143
R-Value Observed: 0.145
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 44.611	α = 90
b = 75.153	β = 97.89
c = 68.206	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
SBC-Collect	data collection
HKL-3000	data reduction
HKL-3000	data scaling
SHELXD	phasing
MLPHARE	phasing
DM	phasing
RESOLVE	phasing
HKL-3000	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2008-09-30

Deposition Author(s):

Midwest Center for Structural Genomics (MCSG)

Revision History (Full details and data files)

Version 1.0: 2008-09-30
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.