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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1M63

Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0033192molecular_functioncalmodulin-dependent protein phosphatase activity
A0097720biological_processcalcineurin-mediated signaling
B0004721molecular_functionphosphoprotein phosphatase activity
B0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005516molecular_functioncalmodulin binding
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005955cellular_componentcalcineurin complex
B0008597molecular_functioncalcium-dependent protein serine/threonine phosphatase regulator activity
B0019902molecular_functionphosphatase binding
B0019904molecular_functionprotein domain specific binding
B0033173biological_processcalcineurin-NFAT signaling cascade
B0042383cellular_componentsarcolemma
B0045202cellular_componentsynapse
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046872molecular_functionmetal ion binding
B0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
B0098685cellular_componentSchaffer collateral - CA1 synapse
B0098686cellular_componenthippocampal mossy fiber to CA3 synapse
B0098688cellular_componentparallel fiber to Purkinje cell synapse
B0098693biological_processregulation of synaptic vesicle cycle
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099149biological_processregulation of postsynaptic neurotransmitter receptor internalization
B0099170biological_processpostsynaptic modulation of chemical synaptic transmission
B1905665biological_processpositive regulation of calcium ion import across plasma membrane
B1905949biological_processnegative regulation of calcium ion import across plasma membrane
C0000413biological_processprotein peptidyl-prolyl isomerization
C0001933biological_processnegative regulation of protein phosphorylation
C0001934biological_processpositive regulation of protein phosphorylation
C0003723molecular_functionRNA binding
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005178molecular_functionintegrin binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006457biological_processprotein folding
C0006469biological_processnegative regulation of protein kinase activity
C0006915biological_processapoptotic process
C0016018molecular_functioncyclosporin A binding
C0016020cellular_componentmembrane
C0016853molecular_functionisomerase activity
C0019076biological_processviral release from host cell
C0030168biological_processplatelet activation
C0030593biological_processneutrophil chemotaxis
C0030595biological_processleukocyte chemotaxis
C0031982cellular_componentvesicle
C0032148biological_processactivation of protein kinase B activity
C0032873biological_processnegative regulation of stress-activated MAPK cascade
C0032991cellular_componentprotein-containing complex
C0034389biological_processlipid droplet organization
C0034599biological_processcellular response to oxidative stress
C0034774cellular_componentsecretory granule lumen
C0042118biological_processendothelial cell activation
C0043410biological_processpositive regulation of MAPK cascade
C0045069biological_processregulation of viral genome replication
C0045070biological_processpositive regulation of viral genome replication
C0046790molecular_functionvirion binding
C0050714biological_processpositive regulation of protein secretion
C0051082molecular_functionunfolded protein binding
C0051092biological_processpositive regulation of NF-kappaB transcription factor activity
C0060352biological_processcell adhesion molecule production
C0061944biological_processnegative regulation of protein K48-linked ubiquitination
C0070062cellular_componentextracellular exosome
C0070527biological_processplatelet aggregation
C1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
C1903901biological_processnegative regulation of viral life cycle
C1904399molecular_functionheparan sulfate binding
C1904813cellular_componentficolin-1-rich granule lumen
C2001233biological_processregulation of apoptotic signaling pathway
E0016787molecular_functionhydrolase activity
E0033192molecular_functioncalmodulin-dependent protein phosphatase activity
E0097720biological_processcalcineurin-mediated signaling
F0004721molecular_functionphosphoprotein phosphatase activity
F0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
F0005509molecular_functioncalcium ion binding
F0005515molecular_functionprotein binding
F0005516molecular_functioncalmodulin binding
F0005654cellular_componentnucleoplasm
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0005955cellular_componentcalcineurin complex
F0008597molecular_functioncalcium-dependent protein serine/threonine phosphatase regulator activity
F0019902molecular_functionphosphatase binding
F0019904molecular_functionprotein domain specific binding
F0033173biological_processcalcineurin-NFAT signaling cascade
F0042383cellular_componentsarcolemma
F0045202cellular_componentsynapse
F0045944biological_processpositive regulation of transcription by RNA polymerase II
F0046872molecular_functionmetal ion binding
F0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
F0098685cellular_componentSchaffer collateral - CA1 synapse
F0098686cellular_componenthippocampal mossy fiber to CA3 synapse
F0098688cellular_componentparallel fiber to Purkinje cell synapse
F0098693biological_processregulation of synaptic vesicle cycle
F0098794cellular_componentpostsynapse
F0098978cellular_componentglutamatergic synapse
F0099149biological_processregulation of postsynaptic neurotransmitter receptor internalization
F0099170biological_processpostsynaptic modulation of chemical synaptic transmission
F1905665biological_processpositive regulation of calcium ion import across plasma membrane
F1905949biological_processnegative regulation of calcium ion import across plasma membrane
G0000413biological_processprotein peptidyl-prolyl isomerization
G0001933biological_processnegative regulation of protein phosphorylation
G0001934biological_processpositive regulation of protein phosphorylation
G0003723molecular_functionRNA binding
G0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
G0005178molecular_functionintegrin binding
G0005515molecular_functionprotein binding
G0005576cellular_componentextracellular region
G0005615cellular_componentextracellular space
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005886cellular_componentplasma membrane
G0005925cellular_componentfocal adhesion
G0006457biological_processprotein folding
G0006469biological_processnegative regulation of protein kinase activity
G0006915biological_processapoptotic process
G0016018molecular_functioncyclosporin A binding
G0016020cellular_componentmembrane
G0016853molecular_functionisomerase activity
G0019076biological_processviral release from host cell
G0030168biological_processplatelet activation
G0030593biological_processneutrophil chemotaxis
G0030595biological_processleukocyte chemotaxis
G0031982cellular_componentvesicle
G0032148biological_processactivation of protein kinase B activity
G0032873biological_processnegative regulation of stress-activated MAPK cascade
G0032991cellular_componentprotein-containing complex
G0034389biological_processlipid droplet organization
G0034599biological_processcellular response to oxidative stress
G0034774cellular_componentsecretory granule lumen
G0042118biological_processendothelial cell activation
G0043410biological_processpositive regulation of MAPK cascade
G0045069biological_processregulation of viral genome replication
G0045070biological_processpositive regulation of viral genome replication
G0046790molecular_functionvirion binding
G0050714biological_processpositive regulation of protein secretion
G0051082molecular_functionunfolded protein binding
G0051092biological_processpositive regulation of NF-kappaB transcription factor activity
G0060352biological_processcell adhesion molecule production
G0061944biological_processnegative regulation of protein K48-linked ubiquitination
G0070062cellular_componentextracellular exosome
G0070527biological_processplatelet aggregation
G1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
G1903901biological_processnegative regulation of viral life cycle
G1904399molecular_functionheparan sulfate binding
G1904813cellular_componentficolin-1-rich granule lumen
G2001233biological_processregulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 500
ChainResidue
BASP30
BASP32
BSER34
BSER36
BGLU41
site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BASP70
BGLU73
BASP62
BASP64
BASN66
BGLU68
site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 502
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110
site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
AASP118
AASN150
AHIS199
AHIS281
AFE505
site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 505
ChainResidue
AASP90
AHIS92
AASP118
AHIS281
AZN504
site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA F 500
ChainResidue
FASP30
FASP32
FSER34
FSER36
FGLU41
site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA F 501
ChainResidue
FASP62
FASP64
FASN66
FGLU68
FASP70
FGLU73
site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA F 502
ChainResidue
FASP99
FASP101
FASP103
FTYR105
FGLU110
site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA F 503
ChainResidue
FASP140
FASP142
FASP144
FARG146
FGLU151
site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E 504
ChainResidue
EASP118
EASN150
EHIS199
EHIS281
EFE505
site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE E 505
ChainResidue
EASP90
EHIS92
EASP118
EZN504
site_idBC4
Number of Residues20
DetailsBINDING SITE FOR CHAIN D OF CYCLOSPORIN A
ChainResidue
ASER2
ALEU312
ATYR341
ATRP342
APRO344
ATRP352
APHE356
BASN122
CARG55
CPHE60
CGLN63
CGLY72
CALA101
CASN102
CGLN111
CPHE113
CTRP121
CLEU122
CHIS126
CARG148
site_idBC5
Number of Residues21
DetailsBINDING SITE FOR CHAIN H OF CYCLOSPORIN A
ChainResidue
GTRP121
GLEU122
GHIS126
ELEU312
EVAL314
ETYR341
ETRP342
EPRO344
ETRP352
EPHE356
FASN122
FLEU123
GARG55
GPHE60
GGLN63
GGLY72
GALA101
GASN102
GALA103
GGLN111
GPHE113
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
ChainResidueDetails
BASP30-PHE42
BASP62-PHE74
BASP99-LEU111
BASP140-PHE152
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU147-GLU152
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG
ChainResidueDetails
CTYR48-GLY65
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues568
DetailsRegion: {"description":"Catalytic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues18
DetailsRegion: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17502104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues56
DetailsRegion: {"description":"Calcineurin B binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsMotif: {"description":"SAPNY motif","evidences":[{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UUQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Interaction with PxVP motif in substrate","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P63328","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues56
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues70
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues10
DetailsRegion: {"description":"Calcineurin A binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsSite: {"description":"Interaction with PxVP motif in substrates of the catalytic subunit","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q63810","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues312
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed","evidences":[{"source":"PubMed","id":"25489052","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"20364129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25678563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17742","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
AASP121
AHIS151
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
EASP121
EHIS151
site_idMCSA1
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
CARG55electrostatic stabiliser, hydrogen bond donor, steric role
AHIS281metal ligand
CPHE60polar/non-polar interaction, steric role
CGLN63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
CASN102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
CPHE113polar/non-polar interaction, steric role
CLEU122polar/non-polar interaction, steric role
CHIS126polar/non-polar interaction, steric role
AHIS199metal ligand
AARG254transition state stabiliser
site_idMCSA2
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
GARG55electrostatic stabiliser, hydrogen bond donor, steric role
EHIS281metal ligand
GPHE60polar/non-polar interaction, steric role
GGLN63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
GASN102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
GPHE113polar/non-polar interaction, steric role
GLEU122polar/non-polar interaction, steric role
GHIS126polar/non-polar interaction, steric role
EHIS199metal ligand
EARG254transition state stabiliser

246704

PDB entries from 2025-12-24

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