Structure of PDB 6mke Chain A

Receptor sequence
>6mkeA (length=117) Species: 5763 (Naegleria fowleri) [Search protein sequence]
TDWIPISQDQRLKKKIITAGSSDEQPPIGSKVSVHYTGTLTSGKKFDSSL
DRGQPFVFTLGKGEVIRGWDLGVKSMKKGEKSYFEIPSDYAYGNNAIPGL
IPANSTLMFEIELLSWK
3D structure
PDB6mke Crystal Structure of Peptidylprolyl Isomerase from Naegleria fowleri with bound FK506
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y38 F48 D49 I68 Y94 F111
Catalytic site (residue number reindexed from 1) Y36 F46 D47 I66 Y92 F109
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 FK5 A Y38 D49 R54 F58 V67 I68 W71 Y94 Y36 D47 R52 F56 V65 I66 W69 Y92
BS02 FK5 A P100 L102 P98 L100
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0016853 isomerase activity
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6mke, PDBe:6mke, PDBj:6mke
PDBsum6mke
PubMed
UniProtA0A2H4A315

[Back to BioLiP]