6ZMD

Crystal structure of HYPE covalently tethered to BiP bound to AMP-PNP

Summary for 6ZMD

Entry DOI	10.2210/pdb6zmd/pdb
Descriptor	Endoplasmic reticulum chaperone BiP, Protein adenylyltransferase FICD, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (7 entities in total)
Functional Keywords	ampylation, endoplasmic reticulum, fic enzyme, chaperone, post-translational modification, transferase
Biological source	Homo sapiens (Human) More
Total number of polymer chains	2
Total formula weight	98330.51
Authors	Fauser, J.,Gulen, B.,Pett, C.,Hedberg, C.,Itzen, A.,Pogenberg, V. (deposition date: 2020-07-02, release date: 2021-04-14, Last modification date: 2024-01-31)
Primary citation	Fauser, J.,Gulen, B.,Pogenberg, V.,Pett, C.,Pourjafar-Dehkordi, D.,Krisp, C.,Hopfner, D.,Konig, G.,Schluter, H.,Feige, M.J.,Zacharias, M.,Hedberg, C.,Itzen, A. Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD. Nat Commun, 12:2426-2426, 2021 Cited by PubMed: 33893288 DOI: 10.1038/s41467-021-22596-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.64 Å)

Structure validation