PDBsum entry 1a2d

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protein metals Protein-protein interface(s) links
Fatty acid binding protein PDB id
Protein chains
131 a.a. *
_CL ×2
Waters ×40
* Residue conservation analysis
PDB id:
Name: Fatty acid binding protein
Title: Pyridoxamine modified murine adipocyte lipid binding protein
Structure: Adipocyte lipid binding protein. Chain: a, b. Synonym: albp-px. Engineered: yes. Other_details: protein modified by reaction with 5-(2- pyridyldithio)pyridoxamine
Source: Mus musculus. House mouse. Organism_taxid: 10090. Cell: adipocyte. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: see kuang et al., Jacs 118\:10702-10706 (1996)
2.40Å     R-factor:   0.196     R-free:   0.273
Authors: J.Ory,A.Mazhary,H.Kuang,R.Davies,M.Distefano,L.Banaszak
Key ref: J.J.Ory et al. (1998). Structural characterization of two synthetic catalysts based on adipocyte lipid-binding protein. Protein Eng, 11, 253-261. PubMed id: 9680187
29-Dec-97     Release date:   01-Jul-98    
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Protein chains
Pfam   ArchSchema ?
P04117  (FABP4_MOUSE) -  Fatty acid-binding protein, adipocyte
132 a.a.
131 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   3 terms 
  Biological process     cellular response to lithium ion   9 terms 
  Biochemical function     transporter activity     2 terms  


Protein Eng 11:253-261 (1998)
PubMed id: 9680187  
Structural characterization of two synthetic catalysts based on adipocyte lipid-binding protein.
J.J.Ory, A.Mazhary, H.Kuang, R.R.Davies, M.D.Distefano, L.J.Banaszak.
Adipocyte lipid-binding protein (ALBP) is a small (14.5 kDa) 10-stranded beta-barrel protein found in mammalian fat cells. The crystal structures of various holo-forms of ALBP have been solved and show the fatty acid ligand bound in a large (approximately 400 A3) cavity isolated from bulk solvent. Examination of the cavity suggests that it would be a good site for the creation of an artificial catalyst, as numerous well defined crystal structures of ALBP are available and past studies have shown the conformation to be reasonably tolerant to modification and mutagenesis. Previous work has shown ALBP to be a good protein scaffold for exploring enantio- and stereoselective reactions; two constructs, ALBP attached to either a pyridoxamine or a phenanthroline group at C117, have been chemically characterized. Both modified proteins have been crystallized and their structures solved and refined. The X-ray models have been used to examine the origin of the chiral selectivity seen in the products. It is apparent that these covalent adducts reduce the internal cavity volume, sterically limiting substrate interactions with the reactive groups, as well as solvent access to potential intermediates in the reaction pathway.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21480401 P.J.Deuss, R.den Heeten, W.Laan, and P.C.Kamer (2011).
Bioinspired catalyst design and artificial metalloenzymes.
  Chemistry, 17, 4680-4698.  
19675646 Y.Lu, N.Yeung, N.Sieracki, and N.M.Marshall (2009).
Design of functional metalloproteins.
  Nature, 460, 855-862.  
10423455 J.J.Ory, and L.J.Banaszak (1999).
Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1, 8-anilinonaphthalene-8-sulfonate.
  Biophys J, 77, 1107-1116.
PDB code: 2ans
9729737 M.D.Distefano, H.Kuang, D.Qi, and A.Mazhary (1998).
The design of protein-based catalysts using semisynthetic methods.
  Curr Opin Struct Biol, 8, 459-465.  
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