Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5FJB

Cyclophilin A Stabilize HIV-1 Capsid through a Novel Non- canonical Binding Site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016032	biological_process	viral process
B	0016032	biological_process	viral process
C	0000413	biological_process	protein peptidyl-prolyl isomerization
C	0001666	biological_process	response to hypoxia
C	0001933	biological_process	negative regulation of protein phosphorylation
C	0001934	biological_process	positive regulation of protein phosphorylation
C	0003723	molecular_function	RNA binding
C	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
C	0005178	molecular_function	integrin binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005925	cellular_component	focal adhesion
C	0006457	biological_process	protein folding
C	0006469	biological_process	negative regulation of protein kinase activity
C	0006915	biological_process	apoptotic process
C	0016018	molecular_function	cyclosporin A binding
C	0016020	cellular_component	membrane
C	0016853	molecular_function	isomerase activity
C	0019076	biological_process	viral release from host cell
C	0030168	biological_process	platelet activation
C	0030182	biological_process	neuron differentiation
C	0030593	biological_process	neutrophil chemotaxis
C	0030595	biological_process	leukocyte chemotaxis
C	0031982	cellular_component	vesicle
C	0032148	biological_process	activation of protein kinase B activity
C	0032873	biological_process	negative regulation of stress-activated MAPK cascade
C	0032991	cellular_component	protein-containing complex
C	0034389	biological_process	lipid droplet organization
C	0034599	biological_process	cellular response to oxidative stress
C	0034774	cellular_component	secretory granule lumen
C	0035307	biological_process	positive regulation of protein dephosphorylation
C	0042118	biological_process	endothelial cell activation
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0043410	biological_process	positive regulation of MAPK cascade
C	0045069	biological_process	regulation of viral genome replication
C	0045070	biological_process	positive regulation of viral genome replication
C	0046790	molecular_function	virion binding
C	0050714	biological_process	positive regulation of protein secretion
C	0051082	molecular_function	unfolded protein binding
C	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
C	0060352	biological_process	cell adhesion molecule production
C	0061944	biological_process	negative regulation of protein K48-linked ubiquitination
C	0070062	cellular_component	extracellular exosome
C	0070527	biological_process	platelet aggregation
C	1902176	biological_process	negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
C	1903901	biological_process	negative regulation of viral life cycle
C	1904399	molecular_function	heparan sulfate binding
C	1904813	cellular_component	ficolin-1-rich granule lumen
C	2001233	biological_process	regulation of apoptotic signaling pathway

Functional Information from PROSITE/UniProt

site_id	PS00170
Number of Residues	18
Details	CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG

Chain	Residue	Details
C	TYR47-GLY64

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269\|PubMed:25489052, ECO:0000269\|Ref.12, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
C	VAL1
B	SER16

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	LYS27
C	LYS81

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	LYS43
C	LYS75
C	LYS130

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	SER76

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:20068231

Chain	Residue	Details
C	THR92

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:20364129, ECO:0000269\|PubMed:25678563, ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	LYS124

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P17742

Chain	Residue	Details
C	LYS132

site_id	SWS_FT_FI8
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
C	ASN107

site_id	SWS_FT_FI9
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Chain	Residue	Details
C	LYS27

site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS81

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 189

Chain	Residue	Details
C	ARG54	electrostatic stabiliser, hydrogen bond donor, steric role
C	PHE59	polar/non-polar interaction, steric role
C	GLN62	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
C	ASN101	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
C	PHE112	polar/non-polar interaction, steric role
C	LEU121	polar/non-polar interaction, steric role
C	HIS125	polar/non-polar interaction, steric role

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)