8W8V

High-resolution X-ray structure of cellulase Cel6A from Phanerochaete chrysosporium at cryogenic temperature, Enzyme-Product complex

PDB DOI: https://doi.org/10.2210/pdb8W8V/pdb

Classification: HYDROLASE
Organism(s): Phanerodontia chrysosporium
Expression System: Komagataella pastoris
Mutation(s): No

Deposited: 2023-09-04 Released: 2025-03-12
Deposition Author(s): Tachioka, M., Yamaguchi, S., Nakamura, A., Ishida, T., Kusaka, K., Yamada, T., Yano, N., Chatake, T., Tamada, T., Takeda, K., Niwa, S., Tanaka, H., Takahashi, S., Inaka, K., Furubayashi, N., Deguchi, S., Samejima, M., Igarashi, K.
Funding Organization(s): Ministry of Education, Culture, Sports, Science and Technology (Japan), Japan Society for the Promotion of Science (JSPS)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 0.85 ?
R-Value Free:
0.119 (Depositor), 0.118 (DCC)
R-Value Work:
0.105 (Depositor), 0.106 (DCC)

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.0 of the entry. See complete history.

Literature

Deprotonated Arginine Controls a Putative Catalytic Base in Invert-ing Family 6 Glycoside Hydrolase

Tachioka, M., Yamaguchi, S., Nakamura, A., Ishida, T., Kusaka, K., Yamada, T., Yano, N., Chatake, T., Tamada, T., Takeda, K., Niwa, S., Tanaka, H., Takahashi, S., Inaka, K., Furubayashi, N., Deguchi, S., Samejima, M., Igarashi, K.

To be published.

Macromolecule Content

Total Structure Weight: 39.55 kDa
Atom Count: 3,754
Modelled Residue Count: 358
Deposited Residue Count: 358
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Glucanase	A	358	Phanerodontia chrysosporium	Mutation(s): 0 Gene Names: cel6A EC: 3.2.1
UniProt
Find proteins for H3K419 (Phanerodontia chrysosporium) Explore H3K419 Go to UniProtKB: H3K419
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	H3K419
Sequence Annotations Expand
Reference Sequence

Oligosaccharides

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Entity ID: 2
Molecule	Chains	Length	2D Diagram	Glycosylation	3D Interactions
beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(4-4)-alpha-D-glucopyranose	B	3	N/A	N/A	Interactions Focus chain B Interactions & Density Focus chain B

Small Molecules

Ligands 4 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
BGC (Subject of Investigation/LOI) Query on BGC Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A] mmCIF format, chain C [auth A]	C [auth A]	beta-D-glucopyranose C₆ H₁₂ O₆ WQZGKKKJIJFFOK-VFUOTHLCSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]
PEG Query on PEG Download Ideal Coordinates CCD File SDF format, chain F [auth A] SDF format, chain G [auth A] SDF format, chain H [auth A] SDF format, chain I [auth A] MOL2 format, chain F [auth A] MOL2 format, chain G [auth A] MOL2 format, chain H [auth A] MOL2 format, chain I [auth A] mmCIF format, chain F [auth A] mmCIF format, chain G [auth A] mmCIF format, chain H [auth A] mmCIF format, chain I [auth A]	F [auth A], G [auth A], H [auth A], I [auth A]	DI(HYDROXYETHYL)ETHER C₄ H₁₀ O₃ MTHSVFCYNBDYFN-UHFFFAOYSA-N		Interactions Focus chain F [auth A] Focus chain G [auth A] Focus chain H [auth A] Focus chain I [auth A] Interactions & Density Focus chain F [auth A] Focus chain G [auth A] Focus chain H [auth A] Focus chain I [auth A]
CL Query on CL Download Ideal Coordinates CCD File SDF format, chain E [auth A] MOL2 format, chain E [auth A] mmCIF format, chain E [auth A]	E [auth A]	CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M		Interactions Focus chain E [auth A] Interactions & Density Focus chain E [auth A]
NA (Subject of Investigation/LOI) Query on NA Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A] mmCIF format, chain D [auth A]	D [auth A]	SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N		Interactions Focus chain D [auth A] Interactions & Density Focus chain D [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 0.85 ?
R-Value Free: 0.119 (Depositor), 0.118 (DCC)
R-Value Work: 0.105 (Depositor), 0.106 (DCC)

Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( ? )	Angle ( ? )
a = 54.044	α = 90
b = 67.581	β = 90
c = 88.354	γ = 90

Software Package:

Software Name	Purpose
SHELXL	refinement
XDS	data scaling
XDS	data reduction

Structure Validation

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Ligand Structure Quality Assessment

Entry History & Funding Information

Deposition Data

Released Date: 2025-03-12

Deposition Author(s):

Funding Organization	Location	Grant Number
Ministry of Education, Culture, Sports, Science and Technology (Japan)	Japan	18H05494
Japan Society for the Promotion of Science (JSPS)	Japan	23H00341, 19H03013, 18J01906, 15J10657

Revision History (Full details and data files)

Version 1.0: 2025-03-12
Type: Initial release

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8W8V

High-resolution X-ray structure of cellulase Cel6A from Phanerochaete chrysosporium at cryogenic temperature, Enzyme-Product complex

Deprotonated Arginine Controls a Putative Catalytic Base in Invert-ing Family 6 Glycoside Hydrolase

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Entity ID: 2

Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)