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2R2J

crystal structure of human ERp44

Functional Information from GO Data
ChainGOidnamespacecontents
A0003756molecular_functionprotein disulfide isomerase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005789cellular_componentendoplasmic reticulum membrane
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0006457biological_processprotein folding
A0006986biological_processresponse to unfolded protein
A0009100biological_processglycoprotein metabolic process
A0009986cellular_componentcell surface
A0034976biological_processresponse to endoplasmic reticulum stress
A0035580cellular_componentspecific granule lumen
A0045454biological_processcell redox homeostasis
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SIN A 380
ChainResidue
ALYS91
AARG92
AILE155
ATYR205

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 378
ChainResidue
AHIS157
AHOH487

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 379
ChainResidue
AARG30
AASN206

Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. RDEL
ChainResidueDetails
AARG374-LEU377

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cqg
ChainResidueDetails
ASER32
ACYS29

224004

PDB entries from 2024-08-21

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