2NU4

Accommodation of positively-charged residues in a hydrophobic specificity pocket: Crystal structures of SGPB in complex with OMTKY3 variants Lys18I and Arg18I

PDB DOI: https://doi.org/10.2210/pdb2NU4/pdb

Classification: HYDROLASE
Organism(s): Streptomyces griseus, Meleagris gallopavo
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2006-11-08 Released: 2006-11-21
Deposition Author(s): Bateman, K.S., Anderson, S., Lu, W., Qasim, M.A., Laskowski Jr., M., James, M.N.G.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.75 Å
R-Value Work: 0.170
R-Value Observed: 0.170

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Accommodation of positively-charged residues in a hydrophobic specificity pocket: Crystal structures of SGPB in complex with OMTKY3 variants Lys18I and Arg18I

Bateman, K.S., Anderson, S., Lu, W., Qasim, M.A., Laskowski Jr., M., James, M.N.G.

To be published.

Macromolecule Content

Total Structure Weight: 24.25 kDa
Atom Count: 1,891
Modelled Residue Count: 236
Deposited Residue Count: 236
Unique protein chains: 2

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Streptogrisin B, Proteinase B	A [auth E]	185	Streptomyces griseus	Mutation(s): 0 EC: 3.4.21.81
UniProt
Find proteins for P00777 (Streptomyces griseus) Explore P00777 Go to UniProtKB: P00777
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00777
Sequence Annotations Expand
Reference Sequence

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
Ovomucoid	B [auth I]	51	Meleagris gallopavo	Mutation(s): 1
UniProt
Find proteins for P68390 (Meleagris gallopavo) Explore P68390 Go to UniProtKB: P68390
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P68390
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.75 Å
R-Value Work: 0.170
R-Value Observed: 0.170
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 45.452	α = 90
b = 54.689	β = 119.33
c = 45.633	γ = 90

Software Package:

Software Name	Purpose
DIP	data collection
X-PLOR	model building
TNT	refinement
DENZO	data reduction
SCALEPACK	data scaling
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2006-11-21

Deposition Author(s):

Laskowski Jr., M.

Revision History (Full details and data files)

Version 1.0: 2006-11-21
Type: Initial release
Version 1.1: 2008-04-29
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2021-10-20
Changes: Database references
Version 1.4: 2023-08-30
Changes: Data collection, Refinement description

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.