3U0G

Crystal structure of branched-chain amino acid aminotransferase from burkholderia pseudomallei

PDB DOI: https://doi.org/10.2210/pdb3U0G/pdb

Classification: TRANSFERASE
Organism(s): Burkholderia pseudomallei
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2011-09-28 Released: 2011-11-09
Deposition Author(s): Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.230
R-Value Work: 0.192
R-Value Observed: 0.194

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of branched-chain amino acid aminotransferase from burkholderia pseudomallei

Staker, B.L., Gardberg, A., Sankaran, B., Seattle Structural Genomics Center for Infectious Disease

To be published.

Macromolecule Content

Total Structure Weight: 218.99 kDa
Atom Count: 14,643
Modelled Residue Count: 1,797
Deposited Residue Count: 1,968
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Putative branched-chain amino acid aminotransferase IlvE	A, B, C, D, E A, B, C, D, E, F	328	Burkholderia pseudomallei	Mutation(s): 0 Gene Names: ilvE, BPSL0793 EC: 2.6.1.42
UniProt
Find proteins for Q3JVJ9 (Burkholderia pseudomallei (strain 1710b)) Explore Q3JVJ9 Go to UniProtKB: Q3JVJ9
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q3JVJ9
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
PO4 Query on PO4 Download Ideal Coordinates CCD File SDF format, chain G [auth A] SDF format, chain I [auth B] SDF format, chain K [auth C] SDF format, chain N [auth D] SDF format, chain P [auth E] SDF format, chain S [auth F] MOL2 format, chain G [auth A] MOL2 format, chain I [auth B] MOL2 format, chain K [auth C] MOL2 format, chain N [auth D] MOL2 format, chain P [auth E] MOL2 format, chain S [auth F]	G [auth A] I [auth B] K [auth C] N [auth D] P [auth E] G [auth A], I [auth B], K [auth C], N [auth D], P [auth E], S [auth F]	PHOSPHATE ION O₄ P NBIIXXVUZAFLBC-UHFFFAOYSA-K		Interactions Focus chain G [auth A] Focus chain I [auth B] Focus chain K [auth C] Focus chain N [auth D] Focus chain P [auth E] Focus chain S [auth F] Interactions & Density Focus chain G [auth A] Focus chain I [auth B] Focus chain K [auth C] Focus chain N [auth D] Focus chain P [auth E] Focus chain S [auth F]
GOL Query on GOL Download Ideal Coordinates CCD File SDF format, chain L [auth C] SDF format, chain Q [auth E] SDF format, chain T [auth F] MOL2 format, chain L [auth C] MOL2 format, chain Q [auth E] MOL2 format, chain T [auth F]	L [auth C], Q [auth E], T [auth F]	GLYCEROL C₃ H₈ O₃ PEDCQBHIVMGVHV-UHFFFAOYSA-N		Interactions Focus chain L [auth C] Focus chain Q [auth E] Focus chain T [auth F] Interactions & Density Focus chain L [auth C] Focus chain Q [auth E] Focus chain T [auth F]
CL Query on CL Download Ideal Coordinates CCD File SDF format, chain H [auth A] SDF format, chain J [auth B] SDF format, chain M [auth C] SDF format, chain O [auth D] SDF format, chain R [auth E] SDF format, chain U [auth F] MOL2 format, chain H [auth A] MOL2 format, chain J [auth B] MOL2 format, chain M [auth C] MOL2 format, chain O [auth D] MOL2 format, chain R [auth E] MOL2 format, chain U [auth F]	H [auth A] J [auth B] M [auth C] O [auth D] R [auth E] H [auth A], J [auth B], M [auth C], O [auth D], R [auth E], U [auth F]	CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M		Interactions Focus chain H [auth A] Focus chain J [auth B] Focus chain M [auth C] Focus chain O [auth D] Focus chain R [auth E] Focus chain U [auth F] Interactions & Density Focus chain H [auth A] Focus chain J [auth B] Focus chain M [auth C] Focus chain O [auth D] Focus chain R [auth E] Focus chain U [auth F]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.230
R-Value Work: 0.192
R-Value Observed: 0.194
Space Group: C 2 2 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 106.97	α = 90
b = 139.27	β = 90
c = 290.86	γ = 90

Software Package:

Software Name	Purpose
BOS	data collection
PHASER	phasing
REFMAC	refinement
XDS	data reduction
XSCALE	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2011-11-09

Deposition Author(s):

Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Revision History (Full details and data files)

Version 1.0: 2011-11-09
Type: Initial release
Version 1.1: 2023-09-13
Changes: Data collection, Database references, Derived calculations, Refinement description