Structure of PDB 6hmz Chain X Binding Site BS02

Receptor Information
>6hmz Chain X (length=170) Species: 3708 (Brassica napus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANPKVFFDILIGKMKAGRVVMELFADVTPRTADNFRALCTGEKGIGQAGK
ALHYKGSAFHRIIPGFMCQGGDFTRGNGTGGESIYGAKFQDENFKLKHTG
PGILSMANSGPNTNGSQFFICTDKTAWLDGKHVVFGKVVDGYNVVKAMEK
VGSERGVTSEPVVIEDCGEI
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain6hmz Chain X Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6hmz Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus.
Resolution1.98 Å
Binding residue
(original residue number in PDB)
A38 G42 E43 K44 L53
Binding residue
(residue number reindexed from 1)
A37 G41 E42 K43 L52
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R62 F67 Q70 N109 F120 L129 H133
Catalytic site (residue number reindexed from 1) R61 F66 Q69 N108 F119 L128 H132
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0016018 cyclosporin A binding
GO:0046872 metal ion binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
Cellular Component
GO:0005737 cytoplasm

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Biological Process

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Cellular Component
External links
PDB RCSB:6hmz, PDBe:6hmz, PDBj:6hmz
PDBsum6hmz
PubMed31249367
UniProtA0A078GRH6

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