Structure of PDB 2wfj Chain A Binding Site BS01

Receptor Information
>2wfj Chain A (length=172) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQ
KPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHN
KEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIE
NQKTDAASKPFAEVRILSCGEL
Ligand information
>2wfj Chain B (length=11) Species: 29910 (Tolypocladium inflatum) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ALLVTAGLVLA
Receptor-Ligand Complex Structure
Global viewLocal viewStructure 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]
PDB2wfj The Thermodynamic Influence of Trapped Water Molecules on a Protein-Ligand Interaction.
Resolution0.75 Å
Binding residue
(original residue number in PDB)
R67 F72 Q75 G84 A113 N114 R115 Q123 F125 H133 H138
Binding residue
(residue number reindexed from 1)
R62 F67 Q70 G79 A108 N109 R110 Q118 F120 H128 H133
Enzymatic activity
Catalytic site (original residue number in PDB) R67 F72 Q75 N114 F125 L134 H138
Catalytic site (residue number reindexed from 1) R62 F67 Q70 N109 F120 L129 H133
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:2wfj, PDBe:2wfj, PDBj:2wfj
PDBsum2wfj
PubMed19499554
UniProtQ13427|PPIG_HUMAN Peptidyl-prolyl cis-trans isomerase G (Gene Name=PPIG)

[Back to BioLiP]