Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5HSV

X-Ray structure of a CypA-Alisporivir complex at 1.5 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0001933	biological_process	negative regulation of protein phosphorylation
A	0001934	biological_process	positive regulation of protein phosphorylation
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0005178	molecular_function	integrin binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006457	biological_process	protein folding
A	0006469	biological_process	negative regulation of protein kinase activity
A	0006915	biological_process	apoptotic process
A	0016018	molecular_function	cyclosporin A binding
A	0016853	molecular_function	isomerase activity
A	0030168	biological_process	platelet activation
A	0030593	biological_process	neutrophil chemotaxis
A	0030595	biological_process	leukocyte chemotaxis
A	0032148	biological_process	activation of protein kinase B activity
A	0032873	biological_process	negative regulation of stress-activated MAPK cascade
A	0034599	biological_process	cellular response to oxidative stress
A	0042118	biological_process	endothelial cell activation
A	0043410	biological_process	positive regulation of MAPK cascade
A	0045069	biological_process	regulation of viral genome replication
A	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
A	0060352	biological_process	cell adhesion molecule production
A	0061944	biological_process	negative regulation of protein K48-linked ubiquitination
A	0070527	biological_process	platelet aggregation
A	1902176	biological_process	negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A	1904399	molecular_function	heparan sulfate binding
A	2001233	biological_process	regulation of apoptotic signaling pathway
B	0000413	biological_process	protein peptidyl-prolyl isomerization
B	0001933	biological_process	negative regulation of protein phosphorylation
B	0001934	biological_process	positive regulation of protein phosphorylation
B	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
B	0005178	molecular_function	integrin binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006457	biological_process	protein folding
B	0006469	biological_process	negative regulation of protein kinase activity
B	0006915	biological_process	apoptotic process
B	0016018	molecular_function	cyclosporin A binding
B	0016853	molecular_function	isomerase activity
B	0030168	biological_process	platelet activation
B	0030593	biological_process	neutrophil chemotaxis
B	0030595	biological_process	leukocyte chemotaxis
B	0032148	biological_process	activation of protein kinase B activity
B	0032873	biological_process	negative regulation of stress-activated MAPK cascade
B	0034599	biological_process	cellular response to oxidative stress
B	0042118	biological_process	endothelial cell activation
B	0043410	biological_process	positive regulation of MAPK cascade
B	0045069	biological_process	regulation of viral genome replication
B	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
B	0060352	biological_process	cell adhesion molecule production
B	0061944	biological_process	negative regulation of protein K48-linked ubiquitination
B	0070527	biological_process	platelet aggregation
B	1902176	biological_process	negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
B	1904399	molecular_function	heparan sulfate binding
B	2001233	biological_process	regulation of apoptotic signaling pathway
C	0000413	biological_process	protein peptidyl-prolyl isomerization
C	0001933	biological_process	negative regulation of protein phosphorylation
C	0001934	biological_process	positive regulation of protein phosphorylation
C	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
C	0005178	molecular_function	integrin binding
C	0005576	cellular_component	extracellular region
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
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	0016853	molecular_function	isomerase activity
C	0030168	biological_process	platelet activation
C	0030593	biological_process	neutrophil chemotaxis
C	0030595	biological_process	leukocyte chemotaxis
C	0032148	biological_process	activation of protein kinase B activity
C	0032873	biological_process	negative regulation of stress-activated MAPK cascade
C	0034599	biological_process	cellular response to oxidative stress
C	0042118	biological_process	endothelial cell activation
C	0043410	biological_process	positive regulation of MAPK cascade
C	0045069	biological_process	regulation of viral genome replication
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	0070527	biological_process	platelet aggregation
C	1902176	biological_process	negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
C	1904399	molecular_function	heparan sulfate binding
C	2001233	biological_process	regulation of apoptotic signaling pathway
D	0000413	biological_process	protein peptidyl-prolyl isomerization
D	0001933	biological_process	negative regulation of protein phosphorylation
D	0001934	biological_process	positive regulation of protein phosphorylation
D	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
D	0005178	molecular_function	integrin binding
D	0005576	cellular_component	extracellular region
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006457	biological_process	protein folding
D	0006469	biological_process	negative regulation of protein kinase activity
D	0006915	biological_process	apoptotic process
D	0016018	molecular_function	cyclosporin A binding
D	0016853	molecular_function	isomerase activity
D	0030168	biological_process	platelet activation
D	0030593	biological_process	neutrophil chemotaxis
D	0030595	biological_process	leukocyte chemotaxis
D	0032148	biological_process	activation of protein kinase B activity
D	0032873	biological_process	negative regulation of stress-activated MAPK cascade
D	0034599	biological_process	cellular response to oxidative stress
D	0042118	biological_process	endothelial cell activation
D	0043410	biological_process	positive regulation of MAPK cascade
D	0045069	biological_process	regulation of viral genome replication
D	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
D	0060352	biological_process	cell adhesion molecule production
D	0061944	biological_process	negative regulation of protein K48-linked ubiquitination
D	0070527	biological_process	platelet aggregation
D	1902176	biological_process	negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
D	1904399	molecular_function	heparan sulfate binding
D	2001233	biological_process	regulation of apoptotic signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue CL A 201

Chain	Residue
A	GLY162
A	GLN163

site_id	AC2
Number of Residues	5
Details	binding site for residue CL B 201

Chain	Residue
B	ASP9
B	GLY18
B	ARG19
B	HOH360
D	PRO16

site_id	AC3
Number of Residues	1
Details	binding site for residue CL B 202

Chain	Residue
B	LYS91

site_id	AC4
Number of Residues	4
Details	binding site for residue CL C 201

Chain	Residue
C	GLY109
C	SER110
C	GLN111
C	GLY74

site_id	AC5
Number of Residues	14
Details	binding site for residues BMT E 1 and MVA E 11

Chain	Residue
A	ARG55
A	PHE60
A	GLN63
A	ALA101
A	ASN102
A	ALA103
A	PHE113
A	HIS126
A	HOH359
E	ABA2
E	DAM3
E	66E4
E	VAL5
E	MLE10

site_id	AC6
Number of Residues	13
Details	binding site for residues BMT E 1 and ABA E 2

Chain	Residue
A	ARG55
A	GLN63
A	GLY72
A	ALA101
A	ASN102
A	ALA103
A	GLN111
A	HOH359
E	DAM3
E	66E4
E	VAL5
E	MLE10
E	MVA11

site_id	AC7
Number of Residues	7
Details	binding site for residues ABA E 2 and DAM E 3

Chain	Residue
A	GLY72
A	ALA101
A	ASN102
A	ALA103
A	GLN111
E	BMT1
E	66E4

site_id	AC8
Number of Residues	5
Details	binding site for residues DAM E 3 and 66E E 4

Chain	Residue
A	GLY72
E	BMT1
E	ABA2
E	VAL5
E	MLE6

site_id	AC9
Number of Residues	6
Details	binding site for Di-peptide 66E E 4 and VAL E 5

Chain	Residue
A	ARG55
E	BMT1
E	DAM3
E	MLE6
E	HOH101
E	HOH102

site_id	AD1
Number of Residues	7
Details	binding site for Di-peptide VAL E 5 and MLE E 6

Chain	Residue
A	ARG55
E	BMT1
E	66E4
E	ALA7
E	HOH101
E	HOH102
H	MLE6

site_id	AD2
Number of Residues	5
Details	binding site for Di-peptide MLE E 6 and ALA E 7

Chain	Residue
E	66E4
E	VAL5
E	DAL8
E	HOH103
H	MLE6

site_id	AD3
Number of Residues	4
Details	binding site for Di-peptide ALA E 7 and DAL E 8

Chain	Residue
E	MLE6
E	MLE9
E	MLE10
E	HOH103

site_id	AD4
Number of Residues	4
Details	binding site for Di-peptide DAL E 8 and MLE E 9

Chain	Residue
A	PHE60
A	TRP121
E	ALA7
E	MLE10

site_id	AD5
Number of Residues	6
Details	binding site for residues MLE E 9 and MLE E 10

Chain	Residue
A	ARG55
A	PHE60
A	TRP121
E	BMT1
E	DAL8
E	MVA11

site_id	AD6
Number of Residues	10
Details	binding site for residues MLE E 10 and MVA E 11

Chain	Residue
A	ARG55
A	PHE60
A	GLN63
A	ALA101
A	ASN102
A	PHE113
A	HIS126
E	BMT1
E	DAL8
E	MLE9

site_id	AD7
Number of Residues	13
Details	binding site for residues BMT F 1 and MVA F 11

Chain	Residue
B	HIS126
B	HOH364
F	ABA2
F	DAM3
F	66E4
F	VAL5
F	MLE10
B	ARG55
B	GLN63
B	ALA101
B	ASN102
B	ALA103
B	PHE113

site_id	AD8
Number of Residues	14
Details	binding site for residues BMT F 1 and ABA F 2

Chain	Residue
B	ARG55
B	GLN63
B	GLY72
B	ALA101
B	ASN102
B	ALA103
B	GLN111
B	HOH364
F	DAM3
F	66E4
F	VAL5
F	MLE10
F	MVA11
F	HOH102

site_id	AD9
Number of Residues	10
Details	binding site for residues ABA F 2 and DAM F 3

Chain	Residue
B	GLY72
B	ALA101
B	ASN102
B	ALA103
B	GLN111
F	BMT1
F	66E4
F	HOH102
F	HOH103
F	HOH105

site_id	AE1
Number of Residues	7
Details	binding site for residues DAM F 3 and 66E F 4

Chain	Residue
B	GLY72
F	BMT1
F	ABA2
F	VAL5
F	MLE6
F	HOH103
F	HOH105

site_id	AE2
Number of Residues	6
Details	binding site for Di-peptide 66E F 4 and VAL F 5

Chain	Residue
F	BMT1
F	ABA2
F	DAM3
F	MLE6
F	HOH101
F	HOH104

site_id	AE3
Number of Residues	6
Details	binding site for Di-peptide VAL F 5 and MLE F 6

Chain	Residue
F	BMT1
F	66E4
F	ALA7
F	HOH101
F	HOH104
G	MLE6

site_id	AE4
Number of Residues	4
Details	binding site for Di-peptide MLE F 6 and ALA F 7

Chain	Residue
F	66E4
F	VAL5
F	DAL8
G	MLE6

site_id	AE5
Number of Residues	3
Details	binding site for Di-peptide ALA F 7 and DAL F 8

Chain	Residue
F	MLE6
F	MLE9
F	MLE10

site_id	AE6
Number of Residues	4
Details	binding site for Di-peptide DAL F 8 and MLE F 9

Chain	Residue
B	PHE60
B	TRP121
F	ALA7
F	MLE10

site_id	AE7
Number of Residues	6
Details	binding site for residues MLE F 9 and MLE F 10

Chain	Residue
B	ARG55
B	PHE60
B	TRP121
F	BMT1
F	DAL8
F	MVA11

site_id	AE8
Number of Residues	10
Details	binding site for residues MLE F 10 and MVA F 11

Chain	Residue
B	ARG55
B	PHE60
B	GLN63
B	ALA101
B	ASN102
B	PHE113
B	HIS126
F	BMT1
F	DAL8
F	MLE9

site_id	AE9
Number of Residues	13
Details	binding site for residues BMT G 1 and ABA G 2

Chain	Residue
C	ARG55
C	GLN63
C	GLY72
C	ALA101
C	ASN102
C	ALA103
C	GLN111
C	HOH363
G	DAM3
G	66E4
G	VAL5
G	MLE10
G	MVA11

site_id	AF1
Number of Residues	14
Details	binding site for residues BMT G 1 and MVA G 11

Chain	Residue
C	ARG55
C	PHE60
C	GLN63
C	ALA101
C	ASN102
C	ALA103
C	PHE113
C	HIS126
C	HOH363
G	ABA2
G	DAM3
G	66E4
G	VAL5
G	MLE10

site_id	AF2
Number of Residues	9
Details	binding site for residues ABA G 2 and DAM G 3

Chain	Residue
C	GLY72
C	ALA101
C	ASN102
C	ALA103
C	GLN111
G	BMT1
G	66E4
G	VAL5
G	HOH101

site_id	AF3
Number of Residues	6
Details	binding site for residues DAM G 3 and 66E G 4

Chain	Residue
C	GLY72
G	BMT1
G	ABA2
G	VAL5
G	MLE6
G	HOH101

site_id	AF4
Number of Residues	5
Details	binding site for Di-peptide 66E G 4 and VAL G 5

Chain	Residue
G	BMT1
G	DAM3
G	MLE6
G	HOH102
G	HOH103

site_id	AF5
Number of Residues	9
Details	binding site for Di-peptide VAL G 5 and MLE G 6

Chain	Residue
C	HOH351
F	MLE6
G	BMT1
G	DAM3
G	66E4
G	ALA7
G	MLE10
G	HOH102
G	HOH103

site_id	AF6
Number of Residues	8
Details	binding site for Di-peptide MLE G 6 and ALA G 7

Chain	Residue
B	LYS125
B	HOH358
C	HOH351
F	MLE6
G	66E4
G	VAL5
G	DAL8
G	MLE10

site_id	AF7
Number of Residues	5
Details	binding site for Di-peptide ALA G 7 and DAL G 8

Chain	Residue
B	LYS125
B	HOH358
G	MLE6
G	MLE9
G	MLE10

site_id	AF8
Number of Residues	4
Details	binding site for Di-peptide DAL G 8 and MLE G 9

Chain	Residue
C	PHE60
C	TRP121
G	ALA7
G	MLE10

site_id	AF9
Number of Residues	7
Details	binding site for residues MLE G 9 and MLE G 10

Chain	Residue
C	ARG55
C	PHE60
C	TRP121
G	BMT1
G	MLE6
G	DAL8
G	MVA11

site_id	AG1
Number of Residues	11
Details	binding site for residues MLE G 10 and MVA G 11

Chain	Residue
C	ARG55
C	PHE60
C	GLN63
C	ALA101
C	ASN102
C	PHE113
C	HIS126
G	BMT1
G	MLE6
G	DAL8
G	MLE9

site_id	AG2
Number of Residues	12
Details	binding site for residues BMT H 1 and ABA H 2

Chain	Residue
D	ARG55
D	GLN63
D	GLY72
D	ALA101
D	ASN102
D	ALA103
D	GLN111
H	DAM3
H	66E4
H	VAL5
H	MLE10
H	MVA11

site_id	AG3
Number of Residues	13
Details	binding site for residues BMT H 1 and MVA H 11

Chain	Residue
D	ARG55
D	PHE60
D	GLN63
D	ALA101
D	ASN102
D	ALA103
D	PHE113
D	HIS126
H	ABA2
H	DAM3
H	66E4
H	VAL5
H	MLE10

site_id	AG4
Number of Residues	8
Details	binding site for residues ABA H 2 and DAM H 3

Chain	Residue
D	GLY72
D	ALA101
D	ASN102
D	ALA103
D	GLN111
H	BMT1
H	66E4
H	VAL5

site_id	AG5
Number of Residues	7
Details	binding site for Di-peptide 66E H 4 and VAL H 5

Chain	Residue
D	ARG55
H	BMT1
H	DAM3
H	MLE6
H	HOH101
H	HOH102
H	HOH103

site_id	AG6
Number of Residues	11
Details	binding site for Di-peptide VAL H 5 and MLE H 6

Chain	Residue
D	ARG55
D	HOH259
E	MLE6
H	BMT1
H	DAM3
H	66E4
H	ALA7
H	MLE10
H	HOH101
H	HOH102
H	HOH103

site_id	AG7
Number of Residues	7
Details	binding site for Di-peptide MLE H 6 and ALA H 7

Chain	Residue
D	HOH259
E	MLE6
H	66E4
H	VAL5
H	DAL8
H	MLE10
H	HOH104

site_id	AG8
Number of Residues	4
Details	binding site for Di-peptide ALA H 7 and DAL H 8

Chain	Residue
H	MLE6
H	MLE9
H	MLE10
H	HOH104

site_id	AG9
Number of Residues	4
Details	binding site for Di-peptide DAL H 8 and MLE H 9

Chain	Residue
D	PHE60
D	TRP121
H	ALA7
H	MLE10

site_id	AH1
Number of Residues	7
Details	binding site for residues MLE H 9 and MLE H 10

Chain	Residue
D	ARG55
D	PHE60
D	TRP121
H	BMT1
H	MLE6
H	DAL8
H	MVA11

site_id	AH2
Number of Residues	11
Details	binding site for residues MLE H 10 and MVA H 11

Chain	Residue
D	ARG55
D	PHE60
D	GLN63
D	ALA101
D	ASN102
D	PHE113
D	HIS126
H	BMT1
H	MLE6
H	DAL8
H	MLE9

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
A	TYR48-GLY65

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	624
Details	Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed","evidences":[{"source":"UniProtKB","id":"P62937","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62937","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62937","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62937","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62937","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17742","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62937","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P62937","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)