1qnm

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1qnm, resolution 2.3Å

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HUMAN MANGANESE SUPEROXIDE DISMUTASE MUTANT Q143N

Overview

Structural and biochemical characterization of the nonliganding residue, glutamine 143 near the manganese of human Mn superoxide dismutase, (hMnSOD), a homotetramer of 22 kDa, reveals a functional role for this, residue. In the wild-type protein, the side-chain amide group of Gln 143, is about 5 A from the metal and is hydrogen-bonded to Tyr 34, which is a, second prominent side chain adjacent to the metal. We have prepared the, site-specific mutant of hMnSOD with the conservative replacement of Gln, 143 --> Asn (Q143N). The crystal structure of Q143N shows that the, side-chain amide nitrogen of residue 143 is 1.7 A more distant from the, manganese than in the wild-type enzyme. The Tyr 34 side-chain hydroxyl in, Q143N is also moved to become 0.6 A more distant from the metal due to an, ... [(full description)]

About this Structure

1QNM is a [Single protein] structure of sequence from [Homo sapiens] with MN as [ligand]. Active as [[1]], with EC number [1.15.1.1]. Full crystallographic information is available from [OCA].

Reference

Probing the active site of human manganese superoxide dismutase: the role of glutamine 143., Hsieh Y, Guan Y, Tu C, Bratt PJ, Angerhofer A, Lepock JR, Hickey MJ, Tainer JA, Nick HS, Silverman DN, Biochemistry. 1998 Apr 7;37(14):4731-9. PMID:9537988

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