1KXJ | pdb_00001kxj

The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima

PDB DOI: https://doi.org/10.2210/pdb1KXJ/pdb

Classification: TRANSFERASE
Organism(s): Thermotoga maritima
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2002-01-31 Released: 2002-03-20
Deposition Author(s): Korolev, S., Skarina, T., Evdokimova, E., Beasley, S., Edwards, A., Joachimiak, A., Savchenko, A., Midwest Center for Structural Genomics (MCSG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free:
0.274 (Depositor), 0.280 (DCC)
R-Value Work:
0.229 (Depositor), 0.230 (DCC)
R-Value Observed:
0.229 (Depositor)

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Crystal structure of glutamine amidotransferase from Thermotoga maritima

Korolev, S., Skarina, T., Evdokimova, E., Beasley, S., Edwards, A., Joachimiak, A., Savchenko, A.

(2002) Proteins 49: 420-422

PubMed: 12360532 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1002/prot.10161
Primary Citation of Related Structures:
1KXJ

Organizational Affiliation

Biosciences Division and Structural Biology Center, Argonne National Laboratory, Argonne, Illinois 60439, USA.

Macromolecule Content

Total Structure Weight: 47.51 kDa
Atom Count: 3,282
Modelled Residue Count: 404
Deposited Residue Count: 410
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Amidotransferase hisH	A, B	205	Thermotoga maritima	Mutation(s): 0 Gene Names: HISH EC: 2.4.2 (PDB Primary Data), 4.3.2.10 (UniProt), 3.5.1.2 (UniProt)
UniProt
Find proteins for Q9X0C8 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)) Explore Q9X0C8 Go to UniProtKB: Q9X0C8
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9X0C8
Sequence Annotations Expand
Reference Sequence LOADING

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
PO4 Query on PO4 Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth A] SDF format, chain E [auth A] SDF format, chain F [auth A] SDF format, chain G [auth B] SDF format, chain H [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth A] MOL2 format, chain E [auth A] MOL2 format, chain F [auth A] MOL2 format, chain G [auth B] MOL2 format, chain H [auth B] mmCIF format, chain C [auth A] mmCIF format, chain D [auth A] mmCIF format, chain E [auth A] mmCIF format, chain F [auth A] mmCIF format, chain G [auth B] mmCIF format, chain H [auth B]	C [auth A] D [auth A] E [auth A] F [auth A] G [auth B] C [auth A], D [auth A], E [auth A], F [auth A], G [auth B], H [auth B]	PHOSPHATE ION O₄ P NBIIXXVUZAFLBC-UHFFFAOYSA-K		Interactions Focus chain C [auth A] Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain G [auth B] Focus chain H [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain G [auth B] Focus chain H [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.274 (Depositor), 0.280 (DCC)
R-Value Work: 0.229 (Depositor), 0.230 (DCC)
R-Value Observed: 0.229 (Depositor)

Space Group: P 3₂ 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 82.045	α = 90
b = 82.045	β = 90
c = 176.352	γ = 120

Software Package:

Software Name	Purpose
d*TREK	data scaling
HKL-2000	data reduction
SnB	phasing
SOLVE	phasing
RESOLVE	model building
O	model building
CNS	refinement
d*TREK	data reduction
HKL-2000	data scaling
RESOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2002-03-20

Deposition Author(s):

Midwest Center for Structural Genomics (MCSG)

Revision History (Full details and data files)

Version 1.0: 2002-03-20
Type: Initial release
Version 1.1: 2008-04-27
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2017-10-11
Changes: Refinement description
Version 1.4: 2024-02-14
Changes: Data collection, Database references, Derived calculations

Prepare Data

Validate Data

Deposit Data

Help and Resources

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The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima

Crystal structure of glutamine amidotransferase from Thermotoga maritima

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)

1KXJ | pdb_00001kxj