Structure of PDB 1rmh Chain A Binding Site BS01

Receptor Information

>1rmh Chain A (length=164) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGS
CFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMA
NAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGK
TSKKITIADCGQLE

Ligand information

>1rmh Chain C (length=6) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

cAAPFc

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1rmh Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization.
Resolution	2.4 Å
Binding residue (original residue number in PDB)	R55 F60 Q63 N102 Q111 F113 W121 L122 H126 R148
Binding residue (residue number reindexed from 1)	R54 F59 Q62 N101 Q110 F112 W120 L121 H125 R147

Enzymatic activity

Catalytic site (original residue number in PDB)	R55 F60 Q63 N102 F113 L122 H126
Catalytic site (residue number reindexed from 1)	R54 F59 Q62 N101 F112 L121 H125
Enzyme Commision number	5.2.1.8: peptidylprolyl isomerase.

Gene Ontology

	Molecular Function
GO:0003723	RNA binding
GO:0003755	peptidyl-prolyl cis-trans isomerase activity
GO:0005178	integrin binding
GO:0005515	protein binding
GO:0016018	cyclosporin A binding
GO:0046790	virion binding
GO:0051082	unfolded protein binding
GO:1904399	heparan sulfate binding

	Biological Process
GO:0000413	protein peptidyl-prolyl isomerization
GO:0001933	negative regulation of protein phosphorylation
GO:0001934	positive regulation of protein phosphorylation
GO:0006457	protein folding
GO:0006469	negative regulation of protein kinase activity
GO:0006915	apoptotic process
GO:0019076	viral release from host cell
GO:0030168	platelet activation
GO:0030182	neuron differentiation
GO:0030593	neutrophil chemotaxis
GO:0030595	leukocyte chemotaxis
GO:0032148	activation of protein kinase B activity
GO:0032873	negative regulation of stress-activated MAPK cascade
GO:0034389	lipid droplet organization
GO:0034599	cellular response to oxidative stress
GO:0042118	endothelial cell activation
GO:0043410	positive regulation of MAPK cascade
GO:0045069	regulation of viral genome replication
GO:0045070	positive regulation of viral genome replication
GO:0050714	positive regulation of protein secretion
GO:0051092	positive regulation of NF-kappaB transcription factor activity
GO:0060352	cell adhesion molecule production
GO:0061944	negative regulation of protein K48-linked ubiquitination
GO:0070527	platelet aggregation
GO:1902176	negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
GO:1903901	negative regulation of viral life cycle
GO:2001233	regulation of apoptotic signaling pathway

	Cellular Component
GO:0005576	extracellular region
GO:0005615	extracellular space
GO:0005634	nucleus
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0005925	focal adhesion
GO:0016020	membrane
GO:0031982	vesicle
GO:0032991	protein-containing complex
GO:0034774	secretory granule lumen
GO:0070062	extracellular exosome
GO:1904813	ficolin-1-rich granule lumen

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Cellular Component

External links

PDB	RCSB:1rmh, PDBe:1rmh, PDBj:1rmh
PDBsum	1rmh
PubMed	8652511
UniProt	P62937\|PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A (Gene Name=PPIA)

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