2CB0

Crystal structure of glucosamine 6-phosphate deaminase from Pyrococcus furiosus

PDB DOI: https://doi.org/10.2210/pdb2CB0/pdb

Classification: ISOMERASE
Organism(s): Pyrococcus furiosus
Expression System: Escherichia coli BL21
Mutation(s): No

Deposited: 2005-12-23 Released: 2007-03-13
Deposition Author(s): Kim, K.J., Kim, M.H., Kang, B.S.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.219
R-Value Work: 0.170
R-Value Observed: 0.172

wwPDB Validation 3D Report Full Report

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

Literature

The Crystal Structure of a Novel Glucosamine-6-Phosphate Deaminase from the Hyperthermophilic Archaeon Pyrococcus Furiosus

Kim, K.J., Kim, M.H., Kim, G., Kang, B.S.

(2007) Proteins 68: 413

PubMed: 17387737 Search on PubMed
DOI: https://doi.org/10.1002/prot.21322
Primary Citation of Related Structures:
2CB0

Organizational Affiliation

Pohang Accelerator Laboratory, POSTECH, Pohang 790-784, Korea.

Macromolecule Content

Total Structure Weight: 76.45 kDa
Atom Count: 5,513
Modelled Residue Count: 653
Deposited Residue Count: 666
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
GLUCOSAMINE-FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE	A, B	333	Pyrococcus furiosus	Mutation(s): 0
UniProt
Find proteins for Q8U3U3 (Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)) Explore Q8U3U3 Go to UniProtKB: Q8U3U3
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q8U3U3
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
GOL Query on GOL Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A]	C [auth A]	GLYCEROL C₃ H₈ O₃ PEDCQBHIVMGVHV-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

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: 1.80 Å
R-Value Free: 0.219
R-Value Work: 0.170
R-Value Observed: 0.172
Space Group: C 2 2 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 61.48	α = 90
b = 93.89	β = 90
c = 200.65	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2007-03-13

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2007-03-13
Type: Initial release
Version 1.1: 2011-05-08
Changes: Version format compliance
Version 1.2: 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.