PDBsum entry 1e5f

Lyase

PDB id: 1e5f

Contents

Protein chains

393 a.a. *

Ligands

PLP ×2

SO4 ×6

GOL

Waters ×645

* Residue conservation analysis

PDB id:

1e5f

Name:

Lyase

Title:

Methionine gamma-lyase (mgl) from trichomonas vaginalis

Structure:

Methionine gamma-lyase. Chain: a, b. Synonym: mgl. Engineered: yes

Source:

Trichomonas vaginalis. Organism_taxid: 412133. Strain: g3. Cellular_location: cytoplasm. Gene: mgl1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Homo-Tetramer (from PDB file)

Resolution:

2.18Å R-factor: 0.162 R-free: 0.212

Authors:

G.Goodall,J.C.Mottram,G.H.Coombs,A.J.Lapthorn

Key ref:

G.Goodall et al. The structure and proposed catalytic mechanism of methionine gamma-Lyase. To be published, .

Date:

25-Jul-00 Release date: 19-Jul-01

Protein chains

O15564  (O15564_TRIVA) -  L-methionine gamma-lyase from Trichomonas vaginalis

Seq: 396 a.a.

Struc: 393 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 1: E.C.4.4.1.1 - cystathionine gamma-lyase.
• Reaction: L,L-cystathionine + H2O = 2-oxobutanoate + L-cysteine + NH4⁺

L,L-cystathionine + H2O = 2-oxobutanoate (Bound ligand (Het Group name = GOL) matches with 62.50% similarity) + L-cysteine + NH4(+)

• Cofactor: Pyridoxal 5'-phosphate

Pyridoxal 5'-phosphate (Bound ligand (Het Group name = PLP) matches with 93.75% similarity)

• Enzyme class 2: E.C.4.4.1.11 - methionine gamma-lyase.
• Reaction: L-methionine + H2O = methanethiol + 2-oxobutanoate + NH4⁺
• Cofactor: Pyridoxal 5'-phosphate

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