Structure of PDB 5ex2 Chain A Binding Site BS02

Receptor Information

>5ex2 Chain A (length=267) Species: 582402 (Hirschia baltica ATCC 49814) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MVEYTKESVQADPENWRSVDPDNLVIFETTKGVVYIELAPEIAPNHVAQI
RKVVRTGLYSGTKFHRVISGFMAQGGDIAATLGREPDLEAVDGEFVFRRD
PKSIVLTVINEEDQTKSQYTGFYNGFPIETRQDELANYSEDKRVESWMPH
CAGVVSMARTNDPNSGKDQFFLMRDESRFLDRKYSSWGRMLEGLDVAKSL
TIGEPPERPDILVSAVMVSDLAPKDRPEAWVMRNDGPMFSLFLDRMGRDK
DVCSLPQTPSVVFVSED

Ligand information

Ligand ID

InChI

InChI=1S/Mg/q+2

InChIKey

JLVVSXFLKOJNIY-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mg+2]
CACTVS 3.341	[Mg++]

Formula

Name

MAGNESIUM ION

PDB chain

5ex2 Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	5ex2 Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.
Resolution	1.294 Å
Binding residue (original residue number in PDB)	G69 R173
Binding residue (residue number reindexed from 1)	G70 R174
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	R65 F70 Q73
Catalytic site (residue number reindexed from 1)	R66 F71 Q74
Enzyme Commision number	5.2.1.8: peptidylprolyl isomerase.

Gene Ontology

	Molecular Function
GO:0003755	peptidyl-prolyl cis-trans isomerase activity
GO:0003824	catalytic activity
GO:0016853	isomerase activity
GO:0046872	metal ion binding

	Biological Process
GO:0000413	protein peptidyl-prolyl isomerization
GO:0006457	protein folding

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Molecular Function

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Biological Process

External links

PDB	RCSB:5ex2, PDBe:5ex2, PDBj:5ex2
PDBsum	5ex2
PubMed	27276069
UniProt	C6XJ17

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