3PH9
Crystal structure of the human anterior gradient protein 3
Summary for 3PH9
| Entry DOI | 10.2210/pdb3ph9/pdb |
| Descriptor | Anterior gradient protein 3 homolog (2 entities in total) |
| Functional Keywords | thioredoxin fold, protein disulfide isomerase, endoplasmic reticulum, isomerase |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted (Probable): Q8TD06 |
| Total number of polymer chains | 2 |
| Total formula weight | 35865.36 |
| Authors | Nguyen, V.D.,Ruddock, L.W.,Salin, M.,Wierenga, R.K. (deposition date: 2010-11-03, release date: 2011-10-19, Last modification date: 2023-09-06) |
| Primary citation | Nguyen, V.D.,Biterova, E.,Salin, M.,Wierenga, R.K.,Ruddock, L.W. Crystal structure of human anterior gradient protein 3. Acta Crystallogr.,Sect.F, 74:425-430, 2018 Cited by PubMed Abstract: Oxidative protein folding in the endoplasmic reticulum is catalyzed by the protein disulfide isomerase family of proteins. Of the 20 recognized human family members, the structures of eight have been deposited in the PDB along with domains from six more. Three members of this family, ERp18, anterior gradient protein 2 (AGR2) and anterior gradient protein 3 (AGR3), are single-domain proteins which share sequence similarity. While ERp18 has a canonical active-site motif and is involved in native disulfide-bond formation, AGR2 and AGR3 lack elements of the active-site motif found in other family members and may both interact with mucins. In order to better define its function, the structure of AGR3 is required. Here, the recombinant expression, purification, crystallization and crystal structure of human AGR3 are described. PubMed: 29969106DOI: 10.1107/S2053230X18009093 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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