PDBsum entry 4x5c

Transferase

PDB id

4x5c

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Contents

			Protein chains

					347 a.a.

			Ligands

					PRP


					POP

			Metals

					_MG ×4

			Waters ×61

PDB id:

4x5c

Links

Name:

Transferase

Title:

Anthranilate phosphoribosyltransferase variant r193l from mycobacterium tuberculosis with pyrophosphate/prpp and mg2+ bound

Structure:

Anthranilate phosphoribosyltransferase. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: trpd. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.33Å

R-factor:

0.200

R-free:

0.256

Authors:

T.V.M.Cookson,E.J.Parker,J.S.Lott

Key ref:

T.V.Cookson et al. (2015). Structures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site. Biochemistry, 54, 6082-6092. PubMed id: 26356348 DOI: 10.1021/acs.biochem.5b00612

Date:

05-Dec-14

Release date:

25-Nov-15

PROCHECK

	Headers

	References

Protein chains

P9WFX5 (TRPD_MYCTU) - Anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: Struc:					370 a.a. 347 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

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



		Enzyme reactions

Enzyme class:

E.C.2.4.2.18 - anthranilate phosphoribosyltransferase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Pathway:

Tryptophan Biosynthesis

Reaction:

N-(5-phospho-beta-D-ribosyl)anthranilate + diphosphate = 5-phospho-alpha- D-ribose 1-diphosphate + anthranilate

N-(5-phospho-beta-D-ribosyl)anthranilate
Bound ligand (Het Group name = PRP)
matches with 40.91% similarity

diphosphate

5-phospho-alpha- D-ribose 1-diphosphate

anthranilate

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

reference

DOI no: 10.1021/acs.biochem.5b00612	Biochemistry 54:6082-6092 (2015)
PubMed id: 26356348

Structures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site.
T.V.Cookson, G.L.Evans, A.Castell, E.N.Baker, J.S.Lott, E.J.Parker.

ABSTRACT

No abstract given.