5GSL

Glycoside hydrolase A

PDB DOI: https://doi.org/10.2210/pdb5GSL/pdb

Classification: HYDROLASE
Organism(s): Pyrococcus horikoshii OT3
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2016-08-16 Released: 2017-02-01
Deposition Author(s): Watanabe, M., Kamachi, S., Mine, S.
Funding Organization(s): The Japan Society for the Promotion of Sciences

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Free: 0.288
R-Value Work: 0.217
R-Value Observed: 0.221

wwPDB Validation 3D Report Full Report

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

Literature

Glycoside hydrolase A

Watanabe, M., Kamachi, S., Mine, S.

To be published.

Macromolecule Content

Total Structure Weight: 182.85 kDa
Atom Count: 13,033
Modelled Residue Count: 1,550
Deposited Residue Count: 1,556
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
778aa long hypothetical beta-galactosidase	A, B	778	Pyrococcus horikoshii OT3	Mutation(s): 0 Gene Names: PH0511
UniProt
Find proteins for O58247 (Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)) Explore O58247 Go to UniProtKB: O58247
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O58247
Sequence Annotations Expand
Reference Sequence

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 B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth A] MOL2 format, chain E [auth B]	C [auth A], D [auth A], E [auth B]	PHOSPHATE ION O₄ P NBIIXXVUZAFLBC-UHFFFAOYSA-K		Interactions Focus chain C [auth A] Focus chain D [auth A] Focus chain E [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth A] Focus chain E [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Free: 0.288
R-Value Work: 0.217
R-Value Observed: 0.221
Space Group: I 2 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 146.843	α = 90
b = 148.767	β = 90
c = 165.69	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
DENZO	data reduction
SCALEPACK	data scaling
PHENIX	phasing

Structure Validation

View Full Validation Report

Entry History & Funding Information

Deposition Data

Released Date: 2017-02-01

Deposition Author(s):

Funding Organization	Location	Grant Number
The Japan Society for the Promotion of Sciences	Japan	25450143

Revision History (Full details and data files)

Version 1.0: 2017-02-01
Type: Initial release
Version 1.1: 2020-02-26
Changes: Data collection
Version 1.2: 2024-03-20
Changes: Data collection, Database references

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.