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1A7X

FKBP12-FK1012 COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003007biological_processheart morphogenesis
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005160molecular_functiontransforming growth factor beta receptor binding
A0005515molecular_functionprotein binding
A0005527molecular_functionmacrolide binding
A0005528molecular_functionFK506 binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0006458biological_process'de novo' protein folding
A0014802cellular_componentterminal cisterna
A0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A0016020cellular_componentmembrane
A0016247molecular_functionchannel regulator activity
A0016529cellular_componentsarcoplasmic reticulum
A0022417biological_processprotein maturation by protein folding
A0030018cellular_componentZ disc
A0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
A0030547molecular_functionsignaling receptor inhibitor activity
A0032092biological_processpositive regulation of protein binding
A0032880biological_processregulation of protein localization
A0032926biological_processnegative regulation of activin receptor signaling pathway
A0033017cellular_componentsarcoplasmic reticulum membrane
A0034713molecular_functiontype I transforming growth factor beta receptor binding
A0042026biological_processprotein refolding
A0042110biological_processT cell activation
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0044325molecular_functiontransmembrane transporter binding
A0050776biological_processregulation of immune response
A0055010biological_processventricular cardiac muscle tissue morphogenesis
A0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
A0060347biological_processheart trabecula formation
A0070411molecular_functionI-SMAD binding
A0070588biological_processcalcium ion transmembrane transport
A0070697molecular_functionactivin receptor binding
A0097435biological_processsupramolecular fiber organization
A0098562cellular_componentcytoplasmic side of membrane
A1902991biological_processregulation of amyloid precursor protein catabolic process
A1990000biological_processamyloid fibril formation
A1990425cellular_componentryanodine receptor complex
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003007biological_processheart morphogenesis
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005160molecular_functiontransforming growth factor beta receptor binding
B0005515molecular_functionprotein binding
B0005527molecular_functionmacrolide binding
B0005528molecular_functionFK506 binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0006458biological_process'de novo' protein folding
B0014802cellular_componentterminal cisterna
B0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
B0016020cellular_componentmembrane
B0016247molecular_functionchannel regulator activity
B0016529cellular_componentsarcoplasmic reticulum
B0022417biological_processprotein maturation by protein folding
B0030018cellular_componentZ disc
B0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
B0030547molecular_functionsignaling receptor inhibitor activity
B0032092biological_processpositive regulation of protein binding
B0032880biological_processregulation of protein localization
B0032926biological_processnegative regulation of activin receptor signaling pathway
B0033017cellular_componentsarcoplasmic reticulum membrane
B0034713molecular_functiontype I transforming growth factor beta receptor binding
B0042026biological_processprotein refolding
B0042110biological_processT cell activation
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0044325molecular_functiontransmembrane transporter binding
B0050776biological_processregulation of immune response
B0055010biological_processventricular cardiac muscle tissue morphogenesis
B0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
B0060347biological_processheart trabecula formation
B0070411molecular_functionI-SMAD binding
B0070588biological_processcalcium ion transmembrane transport
B0070697molecular_functionactivin receptor binding
B0097435biological_processsupramolecular fiber organization
B0098562cellular_componentcytoplasmic side of membrane
B1902991biological_processregulation of amyloid precursor protein catabolic process
B1990000biological_processamyloid fibril formation
B1990425cellular_componentryanodine receptor complex
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FKA B 201
ChainResidue
AGLU54
AASP79
AASP79
AALA81
ATYR82
AHOH320
AHOH404
BTYR26
BPHE36
BASP37
BPHE46
BGLN53
BGLU54
BVAL55
BILE56
BTRP59
BALA81
BTYR82
BPHE99
BHOH391

site_idAP
Number of Residues6
Details
ChainResidue
ATYR26
APHE46
AVAL55
AILE56
ATRP59
APHE99

site_idBP
Number of Residues6
Details
ChainResidue
BILE56
BTRP59
BPHE99
BTYR26
BPHE46
BVAL55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P26883
ChainResidueDetails
AGLN53
BGLN53

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
AILE56
ATYR82
AASP37

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
BILE56
BTYR82
BASP37

site_idMCSA1
Number of Residues6
DetailsM-CSA 362
ChainResidueDetails
ATHR27electrostatic destabiliser, steric role
AASP37electrostatic destabiliser, polar/non-polar interaction, steric role
ASER38electrostatic stabiliser, steric role
AARG57electrostatic stabiliser, steric role
AGLY83electrostatic stabiliser, steric role
AASP100electrostatic destabiliser, polar/non-polar interaction, steric role

site_idMCSA2
Number of Residues6
DetailsM-CSA 362
ChainResidueDetails
BTHR27electrostatic destabiliser, steric role
BASP37electrostatic destabiliser, polar/non-polar interaction, steric role
BSER38electrostatic stabiliser, steric role
BARG57electrostatic stabiliser, steric role
BGLY83electrostatic stabiliser, steric role
BASP100electrostatic destabiliser, polar/non-polar interaction, steric role

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PDB entries from 2024-10-30

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