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Table 1 Conservation of network hydrogen bonds in cyclophilin structures from various species. 3-dimensional structures were aligned using secondary structure elements and equivalent hydrogen bonds were selected based on sequence and structural similarities. Hydrogen bond lengths are in given Å and PDB codes are given in parenthesis [10]. Reprinted with permission from Agarwal et al., Biochemistry (2004) 43, 10605–10618. Copyright (2004) American Chemical Society.

From: Enzymes: An integrated view of structure, dynamics and function

CypA (1AWQ/2CYH/1RMH average) Asp13N-Lys155O Asn35Nδ2-Gly109O Ile56N-Gly150O Ala101N-Gln111O Phe83N-Asn108O
  2.89 3.01 2.96 3.04 2.87
Human Cyclophilin B Gly21N-Asp164O Asn43Nδ2-Gly117O Val64N-Asp159O Ala109N-Gln119O Phe91N-Asn116O
(1CYN) 2.91 3.06 3.00 3.05 2.75
B. malayi Asp16N-Asp167O Asn38Nδ2-Gly120O Val67N-Asn162O Ala112N-Gln122O Phe94N-Asn119O
(1A33) 2.89 2.92 3.05 3.06 2.85
C. elegans Gly13N-Asp162O Asn35Nδ2-Gly116O Ile63N-Gly157O Ala108N-Gln118O Phe90N-Asn115O
Cyclophilin 3 (1DYW) 2.85 3.09 2.96 2.98 2.94
C. elegans Gly37N-Asp180O Asn59Nδ2-Gly133O Val80N-Asp175O Ala125N-Gln135O Phe107N-Asn132O
Cyclophilin 5 (1H0P) 2.78 2.91 2.85 3.09 2.93
B. taurus Gly25N-Leu175O Asn47Nδ2-Gly129O Ile76N-Glu170O Ala121N-Gln131O Phe103N-Asn128O
PPIase (1IHG) 2.98 3.21 2.84 3.07 2.84
P. falciparum Asp14N-Ser162O Asn36Nδ2-Ser116O Ile63N-Gly157O Ala108N-Gln118O Phe90N-Asn115O
Cyclophilin (1QNG) 2.74 2.88 2.93 3.05 2.80
E. coli Asn7N-Ile156O Asn26Nδ2-Thr95O Val44N-Asp149O Ala86N-Gln97O Ile68N-Ala94O
PPIase (2NUL) 2.90 2.67 2.97 2.88 2.76