PDBsum entry 1cwf

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Isomerase/immunosuppressant PDB id
Protein chains
165 a.a. *
11 a.a. *
Waters ×177
* Residue conservation analysis

References listed in PDB file
Key reference
Title X-Ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin a.
Authors J.Kallen, V.Mikol, P.Taylor, M.D.Walkinshaw.
Ref. J Mol Biol, 1998, 283, 435-449. [DOI no: 10.1006/jmbi.1998.2108]
PubMed id 9769216
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 82%.
Eight new X-ray structures of different cyclophilin A/cyclosporin-derivative complexes are presented. These structures, combined with the existing three published cyclosporin complexes, provide a useful structural database for the analysis of protein-ligand interactions. The effect of small chemical differences on protein-ligand hydrogen-bonding, van der Waals interactions and water structure is presented.
Figure 1.
Figure 1. Residue labelling scheme for CsA-analogues (see also Table 1). Atom labelling is according to the IUPAC convention. CN is the methyl carbon atom of the N-methylated amino acids. MLE for MeLeu; MVA for MeVal; BMT for MeBmt; ABU for Abu; SAR for Sar; VAL for Val; ALA for Ala; DAL for D-Ala. All amino acid residues with the exception of D-Ala8 (and Sar3) are in the L-configuration.
Figure 5.
Figure 5. Stereo picture of CsA/CypA with the most conserved water molecules. CsA is coloured magenta, CypA is coloured cyan and the 11 water molecules which occur in 10 or 11 of the 11 structures discussed in this paper are shown as labelled yellow spheres. The label corresponds to the number in Table 5 and also to the label of the water molecule in the deposited PDB file. The position of the sphere is the average position of the water molecules from the different structures which all refine to within 0.2 Å of each other.
The above figures are reprinted by permission from Elsevier: J Mol Biol (1998, 283, 435-449) copyright 1998.
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