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4IPZ

SmBz bound to Cyclophilin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0001933biological_processnegative regulation of protein phosphorylation
A0001934biological_processpositive regulation of protein phosphorylation
A0003723molecular_functionRNA binding
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006357biological_processregulation of transcription by RNA polymerase II
A0006457biological_processprotein folding
A0006469biological_processnegative regulation of protein kinase activity
A0006915biological_processapoptotic process
A0016018molecular_functioncyclosporin A binding
A0016020cellular_componentmembrane
A0019076biological_processviral release from host cell
A0030168biological_processplatelet activation
A0030182biological_processneuron differentiation
A0030593biological_processneutrophil chemotaxis
A0030595biological_processleukocyte chemotaxis
A0031982cellular_componentvesicle
A0032148biological_processactivation of protein kinase B activity
A0032873biological_processnegative regulation of stress-activated MAPK cascade
A0032991cellular_componentprotein-containing complex
A0034389biological_processlipid droplet organization
A0034599biological_processcellular response to oxidative stress
A0034774cellular_componentsecretory granule lumen
A0042118biological_processendothelial cell activation
A0043410biological_processpositive regulation of MAPK cascade
A0045069biological_processregulation of viral genome replication
A0045070biological_processpositive regulation of viral genome replication
A0046790molecular_functionvirion binding
A0050714biological_processpositive regulation of protein secretion
A0051082molecular_functionunfolded protein binding
A0051092biological_processpositive regulation of NF-kappaB transcription factor activity
A0060352biological_processcell adhesion molecule production
A0061944biological_processnegative regulation of protein K48-linked ubiquitination
A0070062cellular_componentextracellular exosome
A0070527biological_processplatelet aggregation
A0140839molecular_functionRNA polymerase II CTD heptapeptide repeat P3 isomerase activity
A0140840molecular_functionRNA polymerase II CTD heptapeptide repeat P6 isomerase activity
A1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A1903901biological_processnegative regulation of viral life cycle
A1904399molecular_functionheparan sulfate binding
A1904813cellular_componentficolin-1-rich granule lumen
A2001233biological_processregulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 201
ChainResidue
APHE46
AASN137

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 202
ChainResidue
ALEU17

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR CHAIN B OF SMBZ
ChainResidue
AALA103
APRO105
AGLN111
APHE113
ATRP121
ATRP121
ALEU122
ALYS125
AHIS126
AHOH348
AHOH377
BHOH101
BHOH102
BHOH104
BHOH104
AARG55
APHE60
AGLN63
AGLY72
AALA101
AASN102

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 Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AMET1

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_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
ChainResidueDetails
AVAL2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS28
ALYS82

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS44
ALYS76
ALYS131

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER77

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ATHR93

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS125

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17742
ChainResidueDetails
ALYS133

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN108

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
ALYS28

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS82

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
AARG55electrostatic stabiliser, hydrogen bond donor, steric role
APHE60polar/non-polar interaction, steric role
AGLN63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AASN102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
APHE113polar/non-polar interaction, steric role
ALEU122polar/non-polar interaction, steric role
AHIS126polar/non-polar interaction, steric role

227111

PDB entries from 2024-11-06

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