Structure of PDB 4odk Chain A Binding Site BS02
Receptor Information
>4odk Chain A (length=153) Species:
274
(Thermus thermophilus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
MKVGQDKVVTIRYTLQVEGEVLDQGELSYLHGHRNLIPGLEEALEGREEG
EAFQAHVPAEKAYGPHDPEGVQVVPLSAFPEDAEVVPGAQFYAQDNPMPL
TVVAVEGEEVTVDFNHPLAGKDLDFQVEVVKVREATPEELLHGHAHPSGH
HHH
Ligand information
>4odk Chain C (length=3) Species:
5062
(Aspergillus oryzae) [
Search peptide sequence
] [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
YPH
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
4odk
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
Resolution
1.401 Å
Binding residue
(original residue number in PDB)
Y13 D23 N35 L36 I37 L40 Y63 L121
Binding residue
(residue number reindexed from 1)
Y13 D23 N35 L36 I37 L40 Y63 L118
Enzymatic activity
Enzyme Commision number
5.2.1.8
: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003755
peptidyl-prolyl cis-trans isomerase activity
GO:0046872
metal ion binding
Biological Process
GO:0042026
protein refolding
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:4odk
,
PDBe:4odk
,
PDBj:4odk
PDBsum
4odk
PubMed
27664121
UniProt
Q5SLE7
[
Back to BioLiP
]