PDBsum entry 7o4t

Oxidoreductase

PDB id: 7o4t

Contents

Protein chains

729 a.a.

402 a.a.

Ligands

COA ×6

GOL ×3

PAP ×2

SO4 ×27

Waters ×265

PDB id:

7o4t

Name:

Oxidoreductase

Title:

Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme with coenzyme a bound at the hydratase, thiolase active sites and possible additional binding site (coa(ech/had))

Structure:

3-hydroxyacyl-coa dehydrogenase. Chain: a, b. Engineered: yes. Putative acyltransferase rv0859. Chain: c, d. Engineered: yes

Source:

Mycobacterium tuberculosis h37rv. Organism_taxid: 83332. Gene: fadb, rv0860. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Mycobacterium tuberculosis (strain atcc 25618 / h37rv). Strain: atcc 25618 / h37rv. Gene: fada, rv0859.

Resolution:

2.10Å R-factor: 0.207 R-free: 0.234

Authors:

S.Dalwani,R.K.Wierenga,R.Venkatesan

Key ref:

S.Dalwani et al. (2021). Substrate specificity and conformational flexibility properties of the mycobacterium tuberculosis beta-Oxi trifunctional enzyme.. J struct biol, 213, 07776. PubMed id: 34371166

Date:

07-Apr-21 Release date: 25-Aug-21

Protein chains

O53872  (O53872_MYCTU) -  Probable fatty oxidation protein FadB from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: 720 a.a.

Struc: 729 a.a.

Protein chains

O53871  (Y0859_MYCTU) -  Putative acyltransferase Rv0859 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: 403 a.a.

Struc: 402 a.a.

Enzyme reactions

• Enzyme class 1: Chains A, B: E.C.1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase.
• Reaction: a (3S)-3-hydroxyacyl-CoA + NAD⁺ = a 3-oxoacyl-CoA + NADH + H⁺

(3S)-3-hydroxyacyl-CoA (Bound ligand (Het Group name = COA) matches with 88.89% similarity) + NAD(+) = 3-oxoacyl-CoA + NADH + H(+)

• Enzyme class 2: Chains C, D: E.C.2.3.1.- - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site