1zk7 Summary


Crystal Structure of Tn501 MerA

The structure was published by Ledwidge, R., Patel, B., Dong, A., et al., Summers, A.O., Pai, E.F., and Miller, S.M., in 2005 in a paper entitled "NmerA, the Metal Binding Domain of Mercuric Ion Reductase, Removes Hg(2+) from Proteins, Delivers It to the Catalytic Core, and Protects Cells under Glutathione-Depleted Conditions" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Mercuric reductase. This molecule has the UniProt identifier P00392 (MERA_PSEAI)search. The sample contained 467 residues which is < 90% of the natural sequence. Out of 467 residues 467 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 homodimers.

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 Mercuric reductase P00392 (96-561) (MERA_PSEAI)search Pseudomonas aeruginosasearch < 90% 467 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00392 (96 - 561) Mercuric reductase Pseudomonas aeruginosa

Chain Sequence family (Pfam)
A Pyridine nucleotide-disulphide oxidoreductase, dimerisation domainsearch, Pyridine nucleotide-disulphide oxidoreductasesearch

Chain ID Biological process (GO) Molecular function (GO)
A (P00392) oxidation-reduction processsearch detoxification of mercury ionsearch cell redox homeostasissearch mercury (II) reductase activitysearch oxidoreductase activitysearch flavin adenine dinucleotide bindingsearch oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptorsearch NADP bindingsearch mercury ion bindingsearch

Chain InterPro annotation
A Mercuric reductasesearch Pyridine nucleotide-disulphide oxidoreductase, NAD-binding domainsearch Pyridine nucleotide-disulphide oxidoreductase, dimerisation domainsearch Pyridine nucleotide-disulphide oxidoreductase, class I, active sitesearch FAD/NAD-linked reductase, dimerisation domainsearch Mercury reductase, MerAsearch Pyridine nucleotide-disulphide oxidoreductase, FAD/NAD(P)-binding domainsearch