SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES DOI:10.2210/pdb1abf/pdb

1ABF   Display Files  close FASTA Sequence PDB File PDB File (Header) mmCIF File mmCIF File (Header) PDBML/XML File PDBML/XML File (Header)   Download Files  close FASTA Sequence PDB File (Text) PDB File (gz) mmCIF File mmCIF File (gz) PDBML/XML File PDBML/XML File (gz) Biological Assembly (gz) (A)   Share this Page  close Facebook Twitter LinkedIn Email Link this Page

Primary Citation       Related Citations in PDB Entry (REMARK 1) Hide     Molecular Description Hide Classification: Binding Protein Structure Weight: 33579.62 Molecule: L-ARABINOSE-BINDING PROTEIN Polymer: 1 Type: protein Length: 306 Chains: A Organism Escherichia coli Gene Names araF b1901 JW1889 UniProtKB:   Protein Feature View | Search PDB | P02924         Source Hide Polymer: 1 Scientific Name: Escherichia coli   Taxonomy         Ligand Chemical Component Hide Identifier Formula Name Interactions FCA Search  Download  C6 H12 O5 ALPHA-D-FUCOSE   Ligand Explorer FCB Search  Download  C6 H12 O5 BETA-D-FUCOSE   Ligand Explorer     External Ligand Annotations Hide Identifier   Binding Affinity (Sequence Identity %) FCA Search  Download  N/A in BindingDB Kd: 3800 nM - data from BindingMOAD   N/A in PDBbind FCB Search  Download  N/A in BindingDB Kd: 3800 nM - data from BindingMOAD   N/A in PDBbind     External Domain Annotations Hide SCOP Classification v1.75: 1 Domain - data from SCOP   CATH Classification v3.4.0: 2 Domains - data from CATH   Pfam Classification: 2 Domains - data from Pfam   GO Terms: 5 Terms - data from GO      Structural Biology Knowledgebase Data Hide     Data in orange boxes are gathered from external resources (when available). Reset Layout

Biological Assembly            View in 3D More Images... Biological assembly 1 assigned by authors Downloadable viewers: Simple Viewer Protein Workshop Ligand Explorer Kiosk Viewer Other Viewers  KiNG WebMol QuickPDB FirstGlance         MyPDB Personal Annotations Hide     Deposition Summary Hide Authors:   Wilson, D.K.,  Quiocho, F.A. Deposition:   1992-04-23 Release:   1993-10-31 Last Modified (REVDAT):   2009-02-24     Revision History    Hide Mouse over text for details 2011-07-13 Version format compliance     Experimental Details Hide Method:   X-RAY DIFFRACTION Exp. Data: N/A Resolution[Å]:   1.90 R-Value: 0.134 (obs.) R-Free: n/a Space Group: P 21 21 21 Unit Cell:   Length [Å] Angles [°] a = 55.92 α = 90.00  b = 72.02 β = 90.00  c = 78.02 γ = 90.00