1nsf Summary



The structure was published by Yu, R.C., Hanson, P.I., Jahn, R., and Brunger, A.T., in 1998 in a paper entitled "Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of N-ETHYLMALEIMIDE SENSITIVE FACTOR. This molecule has the UniProt identifier P18708 (NSF_CRIGR)search. The sample contained 273 residues which is < 90% of the natural sequence. Out of 273 residues 247 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homohexamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A N-ETHYLMALEIMIDE SENSITIVE FACTOR P18708 (478-744) (NSF_CRIGR)search Cricetulus griseussearch < 90% 273 90%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P18708 (478 - 744) N-ETHYLMALEIMIDE SENSITIVE FACTOR Cricetulus griseus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Extended AAA-ATPase domainsearch P-loop containing nucleotide triphosphate hydrolasessearch, Helicase, Ruva Protein; domain 3search ATPase family associated with various cellular activities (AAA)search

Chain ID Molecular function (GO)
A (P18708) nucleotide bindingsearch ATP bindingsearch nucleoside-triphosphatase activitysearch

Chain InterPro annotation
A AAA+ ATPase domainsearch ATPase, AAA-type, coresearch P-loop containing nucleoside triphosphate hydrolasesearch