Structure of PDB 3bo7 Chain A

Receptor sequence
>3bo7A (length=165) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
KKGYLRIVTTQGSLNIELHADMAPRACDSFLRLCAVKYFDDTIFHRCIRN
FMIQGGRAELRQPQSPRSISGFPGGAPFEDEFDNRLVHQGIGVLSMANDG
KHSNLSEFFITFKSCEHLNNKHTIFGRVVGGLDVLRQWEKLETDKKDKPL
KPPKVEEIIVFKNPF
3D structure
PDB3bo7 Crystal Structure of Toxoplasma Gondii Peptidyl-Prolyl Cis-Trans Isomerase, 541.M00136.
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R50 F55 Q58 N109 F120 L129 H133
Catalytic site (residue number reindexed from 1) R46 F51 Q54 N98 F109 L118 H122
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 peptide A R50 F55 M56 Q58 A108 N109 D110 E118 F120 H128 L129 H133 R46 F51 M52 Q54 A97 N98 D99 E107 F109 H117 L118 H122
BS02 peptide A R61 R78 D110 R57 R67 D99
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0061630 ubiquitin protein ligase activity
Biological Process
GO:0000209 protein polyubiquitination
GO:0000413 protein peptidyl-prolyl isomerization
Cellular Component
GO:0071013 catalytic step 2 spliceosome

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3bo7, PDBe:3bo7, PDBj:3bo7
PDBsum3bo7
PubMed
UniProtD0VWS5

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