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2HE9

Structure of the peptidylprolyl isomerase domain of the human NK-tumour recognition protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005975biological_processcarbohydrate metabolic process
A0006457biological_processprotein folding
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005975biological_processcarbohydrate metabolic process
B0006457biological_processprotein folding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 180
ChainResidue
AASN98
APHE99
AILE100
AHOH305
BARG105

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVVknFMiQGG
ChainResidueDetails
ATYR59-GLY76

237735

PDB entries from 2025-06-18

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