PDBsum entry 5kd1

Oxygen transport

PDB id: 5kd1

Contents

Protein chain

153 a.a.

Ligands

HEM

SO4 ×4

3QM

GOL ×5

Waters ×192

PDB id:

5kd1

Name:

Oxygen transport

Title:

Sperm whale myoglobin h64a with nitrosoamphetamine

Structure:

Myoglobin. Chain: a. Engineered: yes. Mutation: yes. Other_details: ala a 64 unp p02185 his 65 engineered mutation asn a 122 unp p02185 asp 123 variant

Source:

Physeter catodon. Sperm whale. Organism_taxid: 9755. Gene: mb. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.70Å R-factor: 0.149 R-free: 0.177

Authors:

B.Wang,Y.Guan,L.M.Thomas,G.B.Richter-Addo

Key ref:

B.Wang et al. (2017). Nitrosoamphetamine binding to myoglobin and hemoglobin: Crystal structure of the H64A myoglobin-nitrosoamphetamine adduct. Nitric Oxide, 67, 26-29. PubMed id: 28450187

Date:

07-Jun-16 Release date: 10-May-17

Protein chain

P02185  (MYG_PHYMC) -  Myoglobin from Physeter macrocephalus

Seq: 154 a.a.

Struc: 153 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Nitric Oxide 67:26-29 (2017)

PubMed id: 28450187

Nitrosoamphetamine binding to myoglobin and hemoglobin: Crystal structure of the H64A myoglobin-nitrosoamphetamine adduct.

B.Wang, S.M.Powell, Y.Guan, N.Xu, L.M.Thomas, G.B.Richter-Addo.

ABSTRACT

N-hydroxyamphetamine (AmphNHOH) is an oxidative metabolite of amphetamine and methamphetamine. It is known to form inhibitory complexes upon binding to heme proteins. However, its interactions with myoglobin (Mb) and hemoglobin (Hb) have not been reported. We demonstrate that the reactions of AmphNHOH with ferric Mb and Hb generate the respective heme-nitrosoamphetamine derivatives characterized by UV-vis spectroscopy. We have determined the X-ray crystal structure of the H64A Mb-nitrosoamphetamine complex to 1.73 Å resolution. The structure reveals the N-binding of the nitroso-d-amphetamine isomer, with no significant H-bonding interactions between the ligand and the distal pocket amino acid residues.