Skip to main content

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