4AL2

peptide deformylase (Ni-form) with hydrosulfide

Summary for 4AL2

Entry DOI	10.2210/pdb4al2/pdb
Related	1BS4 1BS5 1BS6 1BS7 1BS8 1BSJ 1BSK 1BSZ 1DEF 1DFF 1DTF 1G27 1G2A 1ICJ 1LRU 1XEM 1XEN 1XEO 2AI8 2DEF 2DTF 2VHM 2W3T 2W3U 4AL3
Descriptor	PEPTIDE DEFORMYLASE, NICKEL (II) ION, HYDROSULFURIC ACID, ... (4 entities in total)
Functional Keywords	hydrolase, oxidation-reduction
Biological source	ESCHERICHIA COLI
Total number of polymer chains	3
Total formula weight	63963.62
Authors	Palm, G.J.,Hinrichs, W. (deposition date: 2012-02-29, release date: 2012-04-04, Last modification date: 2023-12-20)
Primary citation	Strianese, M.,Palm, G.J.,Milione, S.,Kuehl, O.,Hinrichs, W.,Pellecchia, C. A Fret Enzyme-Based Probe for Monitoring Hydrogen Sulfide. Inorg.Chem., 51:11220-, 2012 Cited by PubMed Abstract: Fluorescently labeled cobalt peptide deformylase (Co-PDF) can be efficiently used as a fluorescence-resonance-energy-transfer-based sensing device for hydrogen sulfide (H(2)S). The proof of concept of our sensor system is substantiated by spectroscopic, structural, and theoretical results. Monohydrogen sulfide coordination to Co-PDF and Ni-PDF was verified by X-ray crystallography. Density functional theory calculations were performed to gain insight into the characteristics of the coordination adduct between H(2)S and the cobalt cofactor in Co-PDF. PubMed: 23072298 DOI: 10.1021/IC301363D PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.6 Å)

Structure validation