6IWE

Crystal structure of fructosyl peptide oxidase thermally stable mutant

PDB DOI: https://doi.org/10.2210/pdb6IWE/pdb

Classification: OXIDOREDUCTASE
Organism(s): Penicillium terrenum
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2018-12-05 Released: 2019-01-02
Deposition Author(s): Fuqing, M., Guangyu, Y.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.94 Å
R-Value Free: 0.252
R-Value Work: 0.208
R-Value Observed: 0.210

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Literature

crystal structure of fructosyl peptide oxidase thermally stable mutant

Fuqiang, M., Guangyu, Y.

To be published.

Macromolecule Content

Total Structure Weight: 49.26 kDa
Atom Count: 3,475
Modelled Residue Count: 430
Deposited Residue Count: 437
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Fructosyl peptide oxidase	A	437	Penicillium terrenum	Mutation(s): 0 Gene Names: fpoxE EC: 1.5.3
UniProt
Find proteins for Q765A9 (Penicillium terrenum) Explore Q765A9 Go to UniProtKB: Q765A9
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q765A9
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FAD Query on FAD Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	FLAVIN-ADENINE DINUCLEOTIDE C₂₇ H₃₃ N₉ O₁₅ P₂ VWWQXMAJTJZDQX-UYBVJOGSSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.94 Å
R-Value Free: 0.252
R-Value Work: 0.208
R-Value Observed: 0.210
Space Group: P 3₂ 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 80.251	α = 90
b = 80.251	β = 90
c = 130.347	γ = 120

Software Package:

Software Name	Purpose
PHENIX	refinement
xia2	data reduction
xia2	data scaling
MOLREP	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2019-01-02

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2019-01-02
Type: Initial release
Version 1.1: 2024-03-27
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.