Structure of PDB 2esl Chain E Binding Site BS01
Receptor Information
>2esl Chain E (length=181) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
RGPSVTAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKGYG
YKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPDENFKLKHYGIGW
VSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQAT
DGHDRPLTNCSIINSGKIDVKTPFVVEIADW
Ligand information
>2esl Chain M (length=11) Species:
29910
(Tolypocladium inflatum) [
Search peptide sequence
] [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
ALLVTPGLVLA
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
2esl
Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
R89 F94 Q97 G106 A135 N136 Q145 F147 W155 H160
Binding residue
(residue number reindexed from 1)
R58 F63 Q66 G75 A104 N105 Q114 F116 W124 H129
Enzymatic activity
Catalytic site (original residue number in PDB)
R89 F94 Q97 N136 F147 L156 H160
Catalytic site (residue number reindexed from 1)
R58 F63 Q66 N105 F116 L125 H129
Enzyme Commision number
5.2.1.8
: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003755
peptidyl-prolyl cis-trans isomerase activity
Biological Process
GO:0000413
protein peptidyl-prolyl isomerization
GO:0006457
protein folding
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:2esl
,
PDBe:2esl
,
PDBj:2esl
PDBsum
2esl
PubMed
20676357
UniProt
P45877
|PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C (Gene Name=PPIC)
[
Back to BioLiP
]