Brand  (β version)

PDB ID: 1APB

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
FCA Alpha-D-fucopyranose PoSSuM
FCB Beta-D-fucopyranose PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1APB   PDBj   RCSB PDB   PDBe
Header : BINDING PROTEINS
Title : A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES
Release Data : 1992-01-15
Compound :
mol_id molecule chains
1 L-ARABINOSE-BINDING PROTEIN A
Source :
mol_id organism_scientific
1 Escherichia coli  (taxid:562)
Authors : Vermersch, P.S., Tesmer, J.J.G., Quiocho, F.A.
Keywords : BINDING PROTEINS
Exp. method : X-RAY DIFFRACTION ( 1.76 Å )
Citation :

A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies.

Vermersch, P.S.,Tesmer, J.J.,Lemon, D.D.  et al.
(1990)  J.Biol.Chem.  265 : 16592 - 16603

PubMed: 2204627

Substrate Specificity and Affinity of a Protein Modulated by Bound Water Molecules

Quiocho, F.A.,Wilson, D.K.,Vyas, N.K.
(1989)  Nature  340 : 404

Novel Stereospecificity of the L-Arabinose-Binding Protein

Quiocho, F.A.,Vyas, N.K.
(1984)  Nature  310 : 381

Hinge-Bending in L-Arabinose-Binding Protein. The "Venus'S-Flytrap" Model

Mao, B.,Pear, M.R.,Mccammon, J.A.  et al.
(1982)  J.Biol.Chem.  257 : 1131

Structure of the L-Arabinose-Binding Protein from Escherichia Coli at 2.4 Angstroms Resolution

Gilliland, G.L.,Quiocho, F.A.
(1981)  J.Mol.Biol.  146 : 341

L-Arabinose-Binding Protein-Sugar Complex at 2.4 Angstroms Resolution. Stereochemistry and Evidence for a Structural Change

Newcomer, M.E.,Gilliand, G.L.,Quiocho, F.A.
(1981)  J.Biol.Chem.  256 : 13213

The Radius of Gyration of L-Arabinose-Binding Protein Decreases Upon Binding of Ligand

Newcomer, M.E.,Lewis, B.A.,Quiocho, F.A.
(1981)  J.Biol.Chem.  256 : 13218

The Thiol Group of the L-Arabinose-Binding Protein. Chromophoric Labeling and Chemical Identification of the Sugar-Binding Site

Miller /III, D.M.,Newcomer, M.E.,Quiocho, F.A.
(1979)  J.Biol.Chem.  254 : 7521

Location of the Sugar-Binding Site of L-Arabinose-Binding Protein. Sugar Derivative Syntheses, Sugar Binding Specificity, and Difference Fourier Analyses

Newcomer, M.E.,Miller /III, D.M.,Quiocho, F.A.
(1979)  J.Biol.Chem.  254 : 7529

The 2.8-Angstroms Resolution Structure of the L-Arabinose-Binding Protein from Escherichia Coli

Quiocho, F.A.,Gilliland, G.L.,Phillips Jr., G.N.
(1977)  J.Biol.Chem.  252 : 5142

Structure of L-Arabinose-Binding Protein from Escherichia Coli at 5 Angstroms Resolution and Preliminary Results at 3.5 Angstroms

Phillips Jr., G.N.,Mahajan, V.K.,Siu, A.K.Q.  et al.
(1976)  Proc.Natl.Acad.Sci.USA  73 : 2186

Reaction

Chain : A
UniProt : P02924 (ARAF_ECOLI)
Reaction : -