5UTO

The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein loaded with palmitic acid to 1.83 Angstrom resolution

PDB DOI: https://doi.org/10.2210/pdb5UTO/pdb

Classification: TRANSPORT PROTEIN
Organism(s): Staphylococcus aureus
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2017-02-15 Released: 2018-02-21
Deposition Author(s): Cuypers, M.G., Ericson, M., Subramanian, C., Broussard, T.C., Miller, D.J., White, S.W., Rock, C.O.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.83 Å
R-Value Free: 0.191
R-Value Work: 0.158
R-Value Observed: 0.160

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.2 of the entry. See complete history.

Literature

The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein loaded with palmitic acid to 1.83 Angstroem resolution

Cuypers, M.G., Ericson, M., Subramanian, C., Broussard, T.C., Miller, D.J., White, S.W., Rock, C.O.

(2018) J Biol Chem

Macromolecule Content

Total Structure Weight: 69.06 kDa
Atom Count: 5,298
Modelled Residue Count: 575
Deposited Residue Count: 616
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
EDD domain protein, DegV family	A, B	308	Staphylococcus aureus	Mutation(s): 0 Gene Names: ERS072738_00223, ERS072840_01626, ERS074020_00218, HMPREF3211_01094
UniProt
Find proteins for P0A0N2 (Staphylococcus aureus) Explore P0A0N2 Go to UniProtKB: P0A0N2
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P0A0N2
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
PLM Query on PLM 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]	PALMITIC ACID C₁₆ H₃₂ O₂ IPCSVZSSVZVIGE-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]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.83 Å
R-Value Free: 0.191
R-Value Work: 0.158
R-Value Observed: 0.160
Space Group: P 1
Diffraction Data: https://doi.org/10.18430/m35uto

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 33.191	α = 105.18
b = 54.289	β = 90.02
c = 84.396	γ = 107.5

Software Package:

Software Name	Purpose
PHENIX	refinement
XDS	data reduction
Aimless	data scaling
PHASER	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2018-02-21

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2018-02-21
Type: Initial release
Version 1.1: 2018-11-21
Changes: Data collection, Database references
Version 1.2: 2023-10-04
Changes: Data collection, Database references, Refinement description

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5UTO

The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein loaded with palmitic acid to 1.83 Angstrom resolution

The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein loaded with palmitic acid to 1.83 Angstroem resolution

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)