4AC1

The structure of a fungal endo-beta-N-acetylglucosaminidase from glycosyl hydrolase family 18, at 1.3A resolution

PDB DOI: https://doi.org/10.2210/pdb4AC1/pdb

Classification: HYDROLASE
Organism(s): Trichoderma reesei
Mutation(s): No

Deposited: 2011-12-12 Released: 2012-08-22
Deposition Author(s): Stals, I., Karkehabadi, S., Devreese, B., Kim, S., Ward, M., Sandgren, M.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.30 Å
R-Value Free: 0.202
R-Value Work: 0.184
R-Value Observed: 0.185

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Macromolecule Content

Total Structure Weight: 32.08 kDa
Atom Count: 2,700
Modelled Residue Count: 283
Deposited Residue Count: 283
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ENDO-N-ACETYL-BETA-D-GLUCOSAMINIDASE	A [auth X]	283	Trichoderma reesei	Mutation(s): 0 EC: 3.2.1.96
UniProt
Find proteins for C4RA89 (Hypocrea jecorina) Explore C4RA89 Go to UniProtKB: C4RA89
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	C4RA89
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
NAG Query on NAG Download Ideal Coordinates CCD File SDF format, chain B [auth X] SDF format, chain C [auth X] MOL2 format, chain B [auth X] MOL2 format, chain C [auth X]	B [auth X], C [auth X]	2-acetamido-2-deoxy-beta-D-glucopyranose C₈ H₁₅ N O₆ OVRNDRQMDRJTHS-FMDGEEDCSA-N		Interactions Focus chain B [auth X] Focus chain C [auth X] Interactions & Density Focus chain B [auth X] Focus chain C [auth X]
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain G [auth X] SDF format, chain H [auth X] SDF format, chain I [auth X] SDF format, chain J [auth X] SDF format, chain K [auth X] SDF format, chain L [auth X] SDF format, chain M [auth X] SDF format, chain N [auth X] MOL2 format, chain G [auth X] MOL2 format, chain H [auth X] MOL2 format, chain I [auth X] MOL2 format, chain J [auth X] MOL2 format, chain K [auth X] MOL2 format, chain L [auth X] MOL2 format, chain M [auth X] MOL2 format, chain N [auth X]	G [auth X] H [auth X] I [auth X] J [auth X] K [auth X] G [auth X], H [auth X], I [auth X], J [auth X], K [auth X], L [auth X], M [auth X], N [auth X]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain G [auth X] Focus chain H [auth X] Focus chain I [auth X] Focus chain J [auth X] Focus chain K [auth X] Focus chain L [auth X] Focus chain M [auth X] Focus chain N [auth X] Interactions & Density Focus chain G [auth X] Focus chain H [auth X] Focus chain I [auth X] Focus chain J [auth X] Focus chain K [auth X] Focus chain L [auth X] Focus chain M [auth X] Focus chain N [auth X]
ACT Query on ACT Download Ideal Coordinates CCD File SDF format, chain D [auth X] SDF format, chain E [auth X] SDF format, chain F [auth X] MOL2 format, chain D [auth X] MOL2 format, chain E [auth X] MOL2 format, chain F [auth X]	D [auth X], E [auth X], F [auth X]	ACETATE ION C₂ H₃ O₂ QTBSBXVTEAMEQO-UHFFFAOYSA-M		Interactions Focus chain D [auth X] Focus chain E [auth X] Focus chain F [auth X] Interactions & Density Focus chain D [auth X] Focus chain E [auth X] Focus chain F [auth X]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.30 Å
R-Value Free: 0.202
R-Value Work: 0.184
R-Value Observed: 0.185
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 35.438	α = 90
b = 63.874	β = 100.97
c = 59.36	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
MOSFLM	data reduction
SCALA	data scaling
PHENIX	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2012-08-22

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2012-08-22
Type: Initial release
Version 1.1: 2018-01-17
Changes: Advisory, Data collection
Version 1.2: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Other, Structure summary

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Help and Resources

4AC1

The structure of a fungal endo-beta-N-acetylglucosaminidase from glycosyl hydrolase family 18, at 1.3A resolution

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)