Structure of PDB 1lop Chain A

Receptor sequence
>1lopA (length=164) Species: 562 (Escherichia coli) [Search protein sequence]
MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMI
QGGGFEPGMKQKATKEPIKNEANNGLKNTRGTLAMARTQAPHSATAQFFI
NVVDNDFLNFSGESLQGWGYCVFAEVVDGMDEVDKIKGVATGRSGMHQDV
PKEDVIIESVTVSE
3D structure
PDB1lop The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R43 F48 Q51 R87 F99 L108 Y120
Catalytic site (residue number reindexed from 1) R43 F48 Q51 R87 F99 L108 Y120
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 R43 I45 F48 A86 R87 Y120 R43 I45 F48 A86 R87 Y120
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0061077 chaperone-mediated protein folding
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Biological Process
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Cellular Component
External links
PDB RCSB:1lop, PDBe:1lop, PDBj:1lop
PDBsum1lop
PubMed8601841
UniProtP23869|PPIB_ECOLI Peptidyl-prolyl cis-trans isomerase B (Gene Name=ppiB)

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