Structure of PDB 5ex2 Chain A

Receptor sequence
>5ex2A (length=267) Species: 582402 (Hirschia baltica ATCC 49814) [Search protein sequence]
MVEYTKESVQADPENWRSVDPDNLVIFETTKGVVYIELAPEIAPNHVAQI
RKVVRTGLYSGTKFHRVISGFMAQGGDIAATLGREPDLEAVDGEFVFRRD
PKSIVLTVINEEDQTKSQYTGFYNGFPIETRQDELANYSEDKRVESWMPH
CAGVVSMARTNDPNSGKDQFFLMRDESRFLDRKYSSWGRMLEGLDVAKSL
TIGEPPERPDILVSAVMVSDLAPKDRPEAWVMRNDGPMFSLFLDRMGRDK
DVCSLPQTPSVVFVSED
3D structure
PDB5ex2 Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.
ChainA
Resolution1.294 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R65 F70 Q73
Catalytic site (residue number reindexed from 1) R66 F71 Q74
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A Q113 Q131 E133 Q114 Q132 E134
BS02 MG A G69 R173 G70 R174
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding

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Molecular Function
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Biological Process
External links
PDB RCSB:5ex2, PDBe:5ex2, PDBj:5ex2
PDBsum5ex2
PubMed27276069
UniProtC6XJ17

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