Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5HKG

Total chemical synthesis, refolding and crystallographic structure of a fully active immunophilin: calstabin 2 (FKBP12.6).

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005102molecular_functionsignaling receptor binding
A0005246molecular_functioncalcium channel regulator activity
A0005515molecular_functionprotein binding
A0005528molecular_functionFK506 binding
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0006458biological_process'de novo' protein folding
A0010459biological_processnegative regulation of heart rate
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A0016020cellular_componentmembrane
A0016529cellular_componentsarcoplasmic reticulum
A0016853molecular_functionisomerase activity
A0019722biological_processcalcium-mediated signaling
A0019855molecular_functioncalcium channel inhibitor activity
A0030018cellular_componentZ disc
A0033017cellular_componentsarcoplasmic reticulum membrane
A0034704cellular_componentcalcium channel complex
A0042026biological_processprotein refolding
A0044325molecular_functiontransmembrane transporter binding
A0050849biological_processnegative regulation of calcium-mediated signaling
A0051280biological_processnegative regulation of release of sequestered calcium ion into cytosol
A0051604biological_processprotein maturation
A0051775biological_processresponse to redox state
A0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue RAP A 201
ChainResidue
AGLU5
AGLN53
AGLU54
AVAL55
AILE56
APHE59
ATYR82
AASP100
AEDO205
AHOH317
AHOH326
ATHR6
AHOH340
AHOH375
AHOH397
ATYR26
ATHR27
AMET29
ALYS35
APHE36
AASP37
APHE46

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 202
ChainResidue
AHIS25
AASN43

site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 203
ChainResidue
ALYS35

site_idAC4
Number of Residues1
Detailsbinding site for residue CL A 204
ChainResidue
AHOH442

site_idAC5
Number of Residues8
Detailsbinding site for residue EDO A 205
ChainResidue
ASER39
AARG42
ALYS44
APHE46
ALYS73
ARAP201
AHOH352
AHOH387

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 206
ChainResidue
ATHR14
AGLN20
ALEU68
AHOH301
AHOH303

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO A 207
ChainResidue
ATYR82
AALA84
ATHR85
AEDO208
AHOH304
AHOH386

site_idAC8
Number of Residues9
Detailsbinding site for residue EDO A 208
ChainResidue
APHE15
APRO78
AASP79
AGLY83
AALA84
AASN94
AEDO207
AHOH304
AHOH310

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues88
DetailsDomain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon