Haem chloroperoxidase structure [1]

PDB	scop	BSM	RELI Base	Header	¹
1cpo	1cpo	1cpo	1cpo	Chloroperoxidase (complex with Mn2+) (modified with N­acetyl­D­glucosamine, ­D­mannose, xylose and ß­L­arabinose; contains cyclised pyroglutamic acid at N­terminus); Caldariomyces fumago	MS6JT6

a	b
	c

¹ Macromolecular Structures abstract. Full text is available to BioMedNet Members

1. Ribbon representation of the Caldariomyces fumago chloroperoxidase (PDB code 1CPO). N­terminal domain (0-98) = green; C­terminal domain (132-298) = violet.
2. Active site structure (orientation as a rotated -20° around x axis): haem; proximal Cys­29; distal side Glu­183 (the proposed acid­base catalyst), water molecule (Wat­801), His­105 and the carbonyl oxygen of Asp­106 form a hydrogen bond network; Phe­186 is supposed to form a part of the substrate access channel.
3. Mn²⁺­binding site structure (orientation as a rotated -45° around x axis). Mn²⁺ ion is octahedrally coordinated by haem propionate, two water molecules (Wat­802 and Wat­803), Glu­103, Ser­108 and the carbonyl oxygen of His­105.

1. Sundaramoorthy, M., Terner, J. and Poulos, T.L. (1995) The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid. Structure 3, 1367-1378.
2. Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24, 946-950.

Bibliography on structural studies of haem chloroperoxidase