1DPD

CRYSTALLOGRAPHIC AND ENZYMATIC INVESTIGATIONS ON THE ROLE OF SER558, HIS610 AND ASN614 IN THE CATALYTIC MECHANISM OF AZOTOBACTER VINELANDII DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P)

Summary for 1DPD

Entry DOI	10.2210/pdb1dpd/pdb
Descriptor	DIHYDROLIPOYL-TRANSACETYLASE (2 entities in total)
Functional Keywords	dihydrolipoamide acetyltransferase
Biological source	Azotobacter vinelandii
Total number of polymer chains	1
Total formula weight	26225.68
Authors	Hendle, J.,Hol, W.G.J. (deposition date: 1995-02-03, release date: 1995-04-20, Last modification date: 2024-02-07)
Primary citation	Hendle, J.,Mattevi, A.,Westphal, A.H.,Spee, J.,de Kok, A.,Teplyakov, A.,Hol, W.G. Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p). Biochemistry, 34:4287-4298, 1995 Cited by PubMed: 7703242 DOI: 10.1021/bi00013a018 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation