Structure of PDB 5xwm Chain B

Receptor sequence
>5xwmB (length=354) Species: 9606 (Homo sapiens) [Search protein sequence]
EITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEF
PNENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSV
KALADYIRQQKSDPIQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFE
RVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVYLGAMTN
FDVTYNWIQDKCVPLVREITFENGEELTEEGLPFLILFHMKEDTESLEIF
QNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHM
YVFGDFKDVLIPGKLKQFVFDLHSGKLHREFHHGPDPTASSPPESSFQKL
APSE
3D structure
PDB5xwm Zinc regulates ERp44-dependent protein quality control in the early secretory pathway.
ChainB
Resolution2.45 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN B H277 H281 H277 H281
BS02 ZN B H299 H328 H332 H299 H328 H332
BS03 ZN B C29 Y78 C29 Y78
Gene Ontology
Molecular Function
GO:0003756 protein disulfide isomerase activity
GO:0005515 protein binding
Biological Process
GO:0006457 protein folding
GO:0006986 response to unfolded protein
GO:0009100 glycoprotein metabolic process
GO:0034976 response to endoplasmic reticulum stress
GO:0045454 cell redox homeostasis
Cellular Component
GO:0005576 extracellular region
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005789 endoplasmic reticulum membrane
GO:0005793 endoplasmic reticulum-Golgi intermediate compartment
GO:0009986 cell surface
GO:0035580 specific granule lumen
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5xwm, PDBe:5xwm, PDBj:5xwm
PDBsum5xwm
PubMed30723194
UniProtQ9BS26|ERP44_HUMAN Endoplasmic reticulum resident protein 44 (Gene Name=ERP44)

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