5ZRT

Crystal structure of human C1ORF123 protein

Summary for 5ZRT

• Entry DOI: 10.2210/pdb5zrt/pdb
• Descriptor: UPF0587 protein C1orf123, GLYCEROL, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: human hypothetical protein, unknown function
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 41312.01

Authors

Rahaman, S.N.A.,Yusop, J.M.,Mohamed-Hussein, Z.A.,Wan Mohd, A.,Ho, K.L.,Teh, A.H.,Waterman, J.,Ng, C.L. (deposition date: 2018-04-25, release date: 2018-08-01, Last modification date: 2023-11-22)

Primary citation

A Rahaman, S.N.,Mat Yusop, J.,Mohamed-Hussein, Z.A.,Aizat, W.M.,Ho, K.L.,Teh, A.H.,Waterman, J.,Tan, B.K.,Tan, H.L.,Li, A.Y.,Chen, E.S.,Ng, C.L.
Crystal structure and functional analysis of human C1ORF123.
Peerj, 6:e5377-e5377, 2018

PubMed Abstract: Proteins of the DUF866 superfamily are exclusively found in eukaryotic cells. A member of the DUF866 superfamily, C1ORF123, is a human protein found in the open reading frame 123 of chromosome 1. The physiological role of C1ORF123 is yet to be determined. The only available protein structure of the DUF866 family shares just 26% sequence similarity and does not contain a zinc binding motif. Here, we present the crystal structure of the recombinant human C1ORF123 protein (rC1ORF123). The structure has a 2-fold internal symmetry dividing the monomeric protein into two mirrored halves that comprise of distinct electrostatic potential. The N-terminal half of rC1ORF123 includes a zinc-binding domain interacting with a zinc ion near to a potential ligand binding cavity. Functional studies of human C1ORF123 and its homologue in the fission yeast (SpEss1) point to a role of DUF866 protein in mitochondrial oxidative phosphorylation.

PubMed: 30280012
DOI: 10.7717/peerj.5377

Experimental method

X-RAY DIFFRACTION (1.9 Å)