Structure of PDB 6hmz Chain X

Receptor sequence
>6hmzX (length=170) Species: 3708 (Brassica napus) [Search protein sequence]
ANPKVFFDILIGKMKAGRVVMELFADVTPRTADNFRALCTGEKGIGQAGK
ALHYKGSAFHRIIPGFMCQGGDFTRGNGTGGESIYGAKFQDENFKLKHTG
PGILSMANSGPNTNGSQFFICTDKTAWLDGKHVVFGKVVDGYNVVKAMEK
VGSERGVTSEPVVIEDCGEI
3D structure
PDB6hmz Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus.
ChainX
Resolution1.98 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 X R62 F67 Q70 G79 A108 N109 S110 Q118 F120 W128 L129 H133 R61 F66 Q69 G78 A107 N108 S109 Q117 F119 W127 L128 H132
BS02 MG X A38 G42 E43 K44 L53 A37 G41 E42 K43 L52
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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Molecular Function
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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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