Phylogenetic analysis indicated that Rv2633c is a member of a distinct subset of hemerythrin-like proteins exclusive to mycobacteria. Primary publication DOI: 10.1042/BCJ20190827. The hemerythrin/HHE cation-binding domain occurs as a duplicated domain in hemerythrins, myohemerythrins and related proteins. I547_5247. This domain binds iron in hemerythrin, but can bind other metals in related proteins, such as cadmium in the Nereis diversicolor hemerythrin. DOI: 10.2210/pdb6q09/pdb. The hemerythrin-like domain family is a repetition of the HHE cation-binding domain, which folds into an up-and-down bundle of four left-handed helices [14,23]. Hemerythrins do not contain heme but use non-heme irons for oxygen transport or PDB Entry - 6U3L (Status - Released) Summary information: Title: Crystal structure of Hemerythrin HHE cation binding domain-containing protein: Rv2633c homolog from Mycobacterium kansasii DOI: 10.2210/pdb6u3l/pdb Primary publication DOI: 10.1042/BCJ20190827 Entry authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) Initial deposition on: 22 August 2019 to be published Release Date 2020-01-22 Peptides Hemerythrin HHE cation binding domain protein: A SMTL:PDB hemerythrin-like protein (HL P) with an HHE (histidine-histidine-glutamic acid) cation-binding domain [7]. The hemerythrin/HHE cation-binding domain occurs as a duplicated domain in hemerythrins, myohemerythrins and related proteins. Hemerythrin HHE cation binding domain protein. Function i Caution. Title: Crystal structure of iron-bound Hemerythrin HHE cation binding domain-containing protein: Rv2633c homolog from Mycobacterium kansasii. Unreviewed-Annotation score: -Experimental evidence at protein level i. Gene. This domain binds iron in hemerythrin, but can bind other metals in related proteins, such as cadmium in the Nereis diversicolor hemerythrin. The HHE cation-binding domain was first predicted by bioinformatics methods as a domain composed of two helical regions and a conserved HHE cation-binding site . These genes were identified as N-acetyltransferases (two genes), putative carboxylesterase, 3-carboxy-cis,cis-muconate cycloisomerase, hemerythrin HHE cation binding domain protein, 3-hydroxyacyl CoA dehydrogenase, putative F420 dependent oxidase, NAD binding protein 3-hydroxylacyl-CoA dehydrogenase, and a putative uncharacterized protein . Entry authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) Initial deposition on: 1 August 2019 Mycobacterium kansasii 824. Abendroth, J. et al., Crystal structure of zinc-bound Hemerythrin HHE cation binding domain-containing protein (soak): Rv2633c homolog from Mycobacterium kansasii. The hemerythrin/HHE cation-binding domain occurs as a duplicated domain in hemerythrins, myohemerythrins and related proteins. This domain binds iron in hemerythrin, but can bind other metals in related proteins, such as cadmium in the Nereis diversicolor hemerythrin. Here, we analyzed the Rv2633c protein sequence, which revealed the presence of an HHE cation-binding domain common in hemerythrin-like proteins. The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. Status. Crystal structure of zinc-bound Hemerythrin HHE cation binding domain-containing protein (soak): Rv2633c homolog from Mycobacterium kansasii: Authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) R / R free: 0.18 / 0.21: Unit cell edges [Å] Furthermore, structural data on hemerythrin‐like domains from two proteins of unknown function, PF0695 from Pyrococcus furiosus and NMB1532 from Neisseria meningitidis, show that the cation‐binding sites, typical of hemerythrin, can be absent or be occupied by metal ions other than iron.