1BEB

BOVINE BETA-LACTOGLOBULIN, LATTICE X

PDB DOI: https://doi.org/10.2210/pdb1BEB/pdb

Classification: LIPOCALIN
Organism(s): Bos taurus
Mutation(s): Yes

Deposited: 1996-12-20 Released: 1997-05-15
Deposition Author(s): Brownlow, S., Morais-Cabral, J.H., Sawyer, L.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.243
R-Value Work: 0.181
R-Value Observed: 0.181

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin.

Brownlow, S., Morais Cabral, J.H., Cooper, R., Flower, D.R., Yewdall, S.J., Polikarpov, I., North, A.C., Sawyer, L.

(1997) Structure 5: 481-495

PubMed: 9115437 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(97)00205-0
Primary Citation of Related Structures:
1BEB

PubMed Abstract:
beta-Lactoglobulin (beta-Lg) is the major whey protein in the milk of ruminants and many other mammals. Its function is not known, but it undergoes at least two pH-dependent conformational changes which may be important. Bovine beta-Lg crystallizes in several different lattices, and medium-resolution structures of orthorhombic lattice Y and trigonal lattice Z have been published. Triclinic lattice X and lattice Z crystals grow at pH values either side of the pH at which one of the pH-induced conformational changes occurs. A full understanding of the structure is needed to help explain both the conformational changes and the different denaturation behaviour of the genetic variants.

Organizational Affiliation

Leeds Centre for Molecular Recognition in Biological Systems, Department of Biochemistry and Molecular Biology, The University of Leeds, Leeds, LS2 9JT, UK.

Macromolecule Content

Total Structure Weight: 36.75 kDa
Atom Count: 2,668
Modelled Residue Count: 312
Deposited Residue Count: 324
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
BETA-LACTOGLOBULIN	A, B	162	Bos taurus	Mutation(s): 1
UniProt
Find proteins for P02754 (Bos taurus) Explore P02754 Go to UniProtKB: P02754
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P02754
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain C [auth B] MOL2 format, chain C [auth B]	C [auth B]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain C [auth B] Interactions & Density Focus chain C [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.243
R-Value Work: 0.181
R-Value Observed: 0.181
Space Group: P 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 37.8	α = 123.4
b = 49.5	β = 97.3
c = 56.6	γ = 103.7

Software Package:

Software Name	Purpose
XDS	data scaling
ROTAVATA	data reduction
Agrovata	data reduction
X-PLOR	model building
X-PLOR	refinement
XDS	data reduction
CCP4	data scaling
ROTAVATA	data scaling
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1997-05-15

Deposition Author(s):

Brownlow, S.

Morais-Cabral, J.H.

Sawyer, L.

Revision History (Full details and data files)

Version 1.0: 1997-05-15
Type: Initial release
Version 1.1: 2008-03-03
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-04-03
Changes: Data collection, Database references, Derived calculations, Refinement description