1a4v

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Image:1a4v.gif

1a4v, resolution 1.8Å

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ALPHA-LACTALBUMIN

Overview

The high-resolution X-ray crystal structure of human alpha-lactalbumin (at, 1.8 A) in the presence of an elevated level of calcium reveals a new, secondary calcium binding site, 7.9 A away from the primary calcium, binding site known in all alpha-lactalbumin structures so far. The new, calcium binding site is different from the zinc and sulfate binding sites, [Ren, J., et al. (1993) J. Biol. Chem. 268, 19292-19298] but shares common, features with the manganese binding site as described by Gerkin [Gerkin, T. A. (1984) Biochemistry 23, 4688-4697]. The proximity of the manganese, and calcium binding region and the location of the functional site on one, side of the charged surface of the alpha-lactalbumin molecule suggest that, these binding sites might play a role in the formation of the lactose, synthase complex.

About this Structure

1A4V is a Single protein structure of sequence from Homo sapiens with CA as ligand. Active as Lactose synthase, with EC number 2.4.1.22 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin., Chandra N, Brew K, Acharya KR, Biochemistry. 1998 Apr 7;37(14):4767-72. PMID:9537992

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