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5HSV

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0001933biological_processnegative regulation of protein phosphorylation
A0001934biological_processpositive regulation of protein phosphorylation
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005178molecular_functionintegrin binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0006469biological_processnegative regulation of protein kinase activity
A0006915biological_processapoptotic process
A0016018molecular_functioncyclosporin A binding
A0030168biological_processplatelet activation
A0030593biological_processneutrophil chemotaxis
A0030595biological_processleukocyte chemotaxis
A0032148biological_processactivation of protein kinase B activity
A0032873biological_processnegative regulation of stress-activated MAPK cascade
A0034599biological_processcellular response to oxidative stress
A0035307biological_processpositive regulation of protein dephosphorylation
A0042118biological_processendothelial cell activation
A0043231cellular_componentintracellular membrane-bounded organelle
A0043410biological_processpositive regulation of MAPK cascade
A0045069biological_processregulation of viral genome replication
A0051092biological_processpositive regulation of NF-kappaB transcription factor activity
A0060352biological_processcell adhesion molecule production
A0061944biological_processnegative regulation of protein K48-linked ubiquitination
A0070527biological_processplatelet aggregation
A1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A1904399molecular_functionheparan sulfate binding
A2001233biological_processregulation of apoptotic signaling pathway
B0000413biological_processprotein peptidyl-prolyl isomerization
B0001933biological_processnegative regulation of protein phosphorylation
B0001934biological_processpositive regulation of protein phosphorylation
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005178molecular_functionintegrin binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0006469biological_processnegative regulation of protein kinase activity
B0006915biological_processapoptotic process
B0016018molecular_functioncyclosporin A binding
B0030168biological_processplatelet activation
B0030593biological_processneutrophil chemotaxis
B0030595biological_processleukocyte chemotaxis
B0032148biological_processactivation of protein kinase B activity
B0032873biological_processnegative regulation of stress-activated MAPK cascade
B0034599biological_processcellular response to oxidative stress
B0035307biological_processpositive regulation of protein dephosphorylation
B0042118biological_processendothelial cell activation
B0043231cellular_componentintracellular membrane-bounded organelle
B0043410biological_processpositive regulation of MAPK cascade
B0045069biological_processregulation of viral genome replication
B0051092biological_processpositive regulation of NF-kappaB transcription factor activity
B0060352biological_processcell adhesion molecule production
B0061944biological_processnegative regulation of protein K48-linked ubiquitination
B0070527biological_processplatelet aggregation
B1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
B1904399molecular_functionheparan sulfate binding
B2001233biological_processregulation of apoptotic signaling pathway
C0000413biological_processprotein peptidyl-prolyl isomerization
C0001933biological_processnegative regulation of protein phosphorylation
C0001934biological_processpositive regulation of protein phosphorylation
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005178molecular_functionintegrin binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006457biological_processprotein folding
C0006469biological_processnegative regulation of protein kinase activity
C0006915biological_processapoptotic process
C0016018molecular_functioncyclosporin A binding
C0030168biological_processplatelet activation
C0030593biological_processneutrophil chemotaxis
C0030595biological_processleukocyte chemotaxis
C0032148biological_processactivation of protein kinase B activity
C0032873biological_processnegative regulation of stress-activated MAPK cascade
C0034599biological_processcellular response to oxidative stress
C0035307biological_processpositive regulation of protein dephosphorylation
C0042118biological_processendothelial cell activation
C0043231cellular_componentintracellular membrane-bounded organelle
C0043410biological_processpositive regulation of MAPK cascade
C0045069biological_processregulation of viral genome replication
C0051092biological_processpositive regulation of NF-kappaB transcription factor activity
C0060352biological_processcell adhesion molecule production
C0061944biological_processnegative regulation of protein K48-linked ubiquitination
C0070527biological_processplatelet aggregation
C1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
C1904399molecular_functionheparan sulfate binding
C2001233biological_processregulation of apoptotic signaling pathway
D0000413biological_processprotein peptidyl-prolyl isomerization
D0001933biological_processnegative regulation of protein phosphorylation
D0001934biological_processpositive regulation of protein phosphorylation
D0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
D0005178molecular_functionintegrin binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006457biological_processprotein folding
D0006469biological_processnegative regulation of protein kinase activity
D0006915biological_processapoptotic process
D0016018molecular_functioncyclosporin A binding
D0030168biological_processplatelet activation
D0030593biological_processneutrophil chemotaxis
D0030595biological_processleukocyte chemotaxis
D0032148biological_processactivation of protein kinase B activity
D0032873biological_processnegative regulation of stress-activated MAPK cascade
D0034599biological_processcellular response to oxidative stress
D0035307biological_processpositive regulation of protein dephosphorylation
D0042118biological_processendothelial cell activation
D0043231cellular_componentintracellular membrane-bounded organelle
D0043410biological_processpositive regulation of MAPK cascade
D0045069biological_processregulation of viral genome replication
D0051092biological_processpositive regulation of NF-kappaB transcription factor activity
D0060352biological_processcell adhesion molecule production
D0061944biological_processnegative regulation of protein K48-linked ubiquitination
D0070527biological_processplatelet aggregation
D1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
D1904399molecular_functionheparan sulfate binding
D2001233biological_processregulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 201
ChainResidue
AGLY162
AGLN163

site_idAC2
Number of Residues5
Detailsbinding site for residue CL B 201
ChainResidue
BASP9
BGLY18
BARG19
BHOH360
DPRO16

site_idAC3
Number of Residues1
Detailsbinding site for residue CL B 202
ChainResidue
BLYS91

site_idAC4
Number of Residues4
Detailsbinding site for residue CL C 201
ChainResidue
CGLY109
CSER110
CGLN111
CGLY74

site_idAC5
Number of Residues14
Detailsbinding site for residues BMT E 1 and MVA E 11
ChainResidue
AARG55
APHE60
AGLN63
AALA101
AASN102
AALA103
APHE113
AHIS126
AHOH359
EABA2
EDAM3
E66E4
EVAL5
EMLE10

site_idAC6
Number of Residues13
Detailsbinding site for residues BMT E 1 and ABA E 2
ChainResidue
AARG55
AGLN63
AGLY72
AALA101
AASN102
AALA103
AGLN111
AHOH359
EDAM3
E66E4
EVAL5
EMLE10
EMVA11

site_idAC7
Number of Residues7
Detailsbinding site for residues ABA E 2 and DAM E 3
ChainResidue
AGLY72
AALA101
AASN102
AALA103
AGLN111
EBMT1
E66E4

site_idAC8
Number of Residues5
Detailsbinding site for residues DAM E 3 and 66E E 4
ChainResidue
AGLY72
EBMT1
EABA2
EVAL5
EMLE6

site_idAC9
Number of Residues6
Detailsbinding site for Di-peptide 66E E 4 and VAL E 5
ChainResidue
AARG55
EBMT1
EDAM3
EMLE6
EHOH101
EHOH102

site_idAD1
Number of Residues7
Detailsbinding site for Di-peptide VAL E 5 and MLE E 6
ChainResidue
AARG55
EBMT1
E66E4
EALA7
EHOH101
EHOH102
HMLE6

site_idAD2
Number of Residues5
Detailsbinding site for Di-peptide MLE E 6 and ALA E 7
ChainResidue
E66E4
EVAL5
EDAL8
EHOH103
HMLE6

site_idAD3
Number of Residues4
Detailsbinding site for Di-peptide ALA E 7 and DAL E 8
ChainResidue
EMLE6
EMLE9
EMLE10
EHOH103

site_idAD4
Number of Residues4
Detailsbinding site for Di-peptide DAL E 8 and MLE E 9
ChainResidue
APHE60
ATRP121
EALA7
EMLE10

site_idAD5
Number of Residues6
Detailsbinding site for residues MLE E 9 and MLE E 10
ChainResidue
AARG55
APHE60
ATRP121
EBMT1
EDAL8
EMVA11

site_idAD6
Number of Residues10
Detailsbinding site for residues MLE E 10 and MVA E 11
ChainResidue
AARG55
APHE60
AGLN63
AALA101
AASN102
APHE113
AHIS126
EBMT1
EDAL8
EMLE9

site_idAD7
Number of Residues13
Detailsbinding site for residues BMT F 1 and MVA F 11
ChainResidue
BHIS126
BHOH364
FABA2
FDAM3
F66E4
FVAL5
FMLE10
BARG55
BGLN63
BALA101
BASN102
BALA103
BPHE113

site_idAD8
Number of Residues14
Detailsbinding site for residues BMT F 1 and ABA F 2
ChainResidue
BARG55
BGLN63
BGLY72
BALA101
BASN102
BALA103
BGLN111
BHOH364
FDAM3
F66E4
FVAL5
FMLE10
FMVA11
FHOH102

site_idAD9
Number of Residues10
Detailsbinding site for residues ABA F 2 and DAM F 3
ChainResidue
BGLY72
BALA101
BASN102
BALA103
BGLN111
FBMT1
F66E4
FHOH102
FHOH103
FHOH105

site_idAE1
Number of Residues7
Detailsbinding site for residues DAM F 3 and 66E F 4
ChainResidue
BGLY72
FBMT1
FABA2
FVAL5
FMLE6
FHOH103
FHOH105

site_idAE2
Number of Residues6
Detailsbinding site for Di-peptide 66E F 4 and VAL F 5
ChainResidue
FBMT1
FABA2
FDAM3
FMLE6
FHOH101
FHOH104

site_idAE3
Number of Residues6
Detailsbinding site for Di-peptide VAL F 5 and MLE F 6
ChainResidue
FBMT1
F66E4
FALA7
FHOH101
FHOH104
GMLE6

site_idAE4
Number of Residues4
Detailsbinding site for Di-peptide MLE F 6 and ALA F 7
ChainResidue
F66E4
FVAL5
FDAL8
GMLE6

site_idAE5
Number of Residues3
Detailsbinding site for Di-peptide ALA F 7 and DAL F 8
ChainResidue
FMLE6
FMLE9
FMLE10

site_idAE6
Number of Residues4
Detailsbinding site for Di-peptide DAL F 8 and MLE F 9
ChainResidue
BPHE60
BTRP121
FALA7
FMLE10

site_idAE7
Number of Residues6
Detailsbinding site for residues MLE F 9 and MLE F 10
ChainResidue
BARG55
BPHE60
BTRP121
FBMT1
FDAL8
FMVA11

site_idAE8
Number of Residues10
Detailsbinding site for residues MLE F 10 and MVA F 11
ChainResidue
BARG55
BPHE60
BGLN63
BALA101
BASN102
BPHE113
BHIS126
FBMT1
FDAL8
FMLE9

site_idAE9
Number of Residues13
Detailsbinding site for residues BMT G 1 and ABA G 2
ChainResidue
CARG55
CGLN63
CGLY72
CALA101
CASN102
CALA103
CGLN111
CHOH363
GDAM3
G66E4
GVAL5
GMLE10
GMVA11

site_idAF1
Number of Residues14
Detailsbinding site for residues BMT G 1 and MVA G 11
ChainResidue
CARG55
CPHE60
CGLN63
CALA101
CASN102
CALA103
CPHE113
CHIS126
CHOH363
GABA2
GDAM3
G66E4
GVAL5
GMLE10

site_idAF2
Number of Residues9
Detailsbinding site for residues ABA G 2 and DAM G 3
ChainResidue
CGLY72
CALA101
CASN102
CALA103
CGLN111
GBMT1
G66E4
GVAL5
GHOH101

site_idAF3
Number of Residues6
Detailsbinding site for residues DAM G 3 and 66E G 4
ChainResidue
CGLY72
GBMT1
GABA2
GVAL5
GMLE6
GHOH101

site_idAF4
Number of Residues5
Detailsbinding site for Di-peptide 66E G 4 and VAL G 5
ChainResidue
GBMT1
GDAM3
GMLE6
GHOH102
GHOH103

site_idAF5
Number of Residues9
Detailsbinding site for Di-peptide VAL G 5 and MLE G 6
ChainResidue
CHOH351
FMLE6
GBMT1
GDAM3
G66E4
GALA7
GMLE10
GHOH102
GHOH103

site_idAF6
Number of Residues8
Detailsbinding site for Di-peptide MLE G 6 and ALA G 7
ChainResidue
BLYS125
BHOH358
CHOH351
FMLE6
G66E4
GVAL5
GDAL8
GMLE10

site_idAF7
Number of Residues5
Detailsbinding site for Di-peptide ALA G 7 and DAL G 8
ChainResidue
BLYS125
BHOH358
GMLE6
GMLE9
GMLE10

site_idAF8
Number of Residues4
Detailsbinding site for Di-peptide DAL G 8 and MLE G 9
ChainResidue
CPHE60
CTRP121
GALA7
GMLE10

site_idAF9
Number of Residues7
Detailsbinding site for residues MLE G 9 and MLE G 10
ChainResidue
CARG55
CPHE60
CTRP121
GBMT1
GMLE6
GDAL8
GMVA11

site_idAG1
Number of Residues11
Detailsbinding site for residues MLE G 10 and MVA G 11
ChainResidue
CARG55
CPHE60
CGLN63
CALA101
CASN102
CPHE113
CHIS126
GBMT1
GMLE6
GDAL8
GMLE9

site_idAG2
Number of Residues12
Detailsbinding site for residues BMT H 1 and ABA H 2
ChainResidue
DARG55
DGLN63
DGLY72
DALA101
DASN102
DALA103
DGLN111
HDAM3
H66E4
HVAL5
HMLE10
HMVA11

site_idAG3
Number of Residues13
Detailsbinding site for residues BMT H 1 and MVA H 11
ChainResidue
DARG55
DPHE60
DGLN63
DALA101
DASN102
DALA103
DPHE113
DHIS126
HABA2
HDAM3
H66E4
HVAL5
HMLE10

site_idAG4
Number of Residues8
Detailsbinding site for residues ABA H 2 and DAM H 3
ChainResidue
DGLY72
DALA101
DASN102
DALA103
DGLN111
HBMT1
H66E4
HVAL5

site_idAG5
Number of Residues7
Detailsbinding site for Di-peptide 66E H 4 and VAL H 5
ChainResidue
DARG55
HBMT1
HDAM3
HMLE6
HHOH101
HHOH102
HHOH103

site_idAG6
Number of Residues11
Detailsbinding site for Di-peptide VAL H 5 and MLE H 6
ChainResidue
DARG55
DHOH259
EMLE6
HBMT1
HDAM3
H66E4
HALA7
HMLE10
HHOH101
HHOH102
HHOH103

site_idAG7
Number of Residues7
Detailsbinding site for Di-peptide MLE H 6 and ALA H 7
ChainResidue
DHOH259
EMLE6
H66E4
HVAL5
HDAL8
HMLE10
HHOH104

site_idAG8
Number of Residues4
Detailsbinding site for Di-peptide ALA H 7 and DAL H 8
ChainResidue
HMLE6
HMLE9
HMLE10
HHOH104

site_idAG9
Number of Residues4
Detailsbinding site for Di-peptide DAL H 8 and MLE H 9
ChainResidue
DPHE60
DTRP121
HALA7
HMLE10

site_idAH1
Number of Residues7
Detailsbinding site for residues MLE H 9 and MLE H 10
ChainResidue
DARG55
DPHE60
DTRP121
HBMT1
HMLE6
HDAL8
HMVA11

site_idAH2
Number of Residues11
Detailsbinding site for residues MLE H 10 and MVA H 11
ChainResidue
DARG55
DPHE60
DGLN63
DALA101
DASN102
DPHE113
DHIS126
HBMT1
HMLE6
HDAL8
HMLE9

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG
ChainResidueDetails
ATYR48-GLY65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
AMET1
BMET1
CMET1
DMET1

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
AVAL2
BVAL2
CVAL2
DVAL2

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ALYS28
ALYS82
BLYS28
BLYS82
CLYS28
CLYS82
DLYS28
DLYS82

site_idSWS_FT_FI4
Number of Residues16
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ALYS44
CLYS76
CLYS125
CLYS131
DLYS44
DLYS76
DLYS125
DLYS131
ALYS76
ALYS125
ALYS131
BLYS44
BLYS76
BLYS125
BLYS131
CLYS44

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ASER77
BSER77
CSER77
DSER77

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ATHR93
BTHR93
CTHR93
DTHR93

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17742
ChainResidueDetails
ALYS133
BLYS133
CLYS133
DLYS133

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN108
BASN108
CASN108
DASN108

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ALYS28
BLYS28
CLYS28
DLYS28

site_idSWS_FT_FI10
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ALYS82
BLYS82
CLYS82
DLYS82

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PDB entries from 2024-07-10

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