PDBsum entry 5k5b

Transferase

PDB id: 5k5b

Contents

Protein chain

306 a.a.

Ligands

ACT ×3

MPD

LBV

Waters ×322

PDB id:

5k5b

Name:

Transferase

Title:

Wild-type pas-gaf fragment from deinococcus radiodurans bphp

Structure:

Bacteriophytochrome. Chain: a. Synonym: phytochrome-like protein. Engineered: yes

Source:

Deinococcus radiodurans. Organism_taxid: 243230. Strain: atcc 13939 / dsm 20539 / jcm 16871 / lmg 4051 / nbrc 15346 / ncimb 9279 / r1 / vkm b-1422. Atcc: 13939. Gene: bphp, dr_a0050. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.35Å R-factor: 0.142 R-free: 0.171

Authors:

H.Takala,P.Edlund,E.Claesson,J.A.Ihalainen,S.Westenhoff

Key ref:

P.Edlund et al. (2016). The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography. Sci Rep, 6, 35279. PubMed id: 27756898 DOI: 10.1038/srep35279

Date:

23-May-16 Release date: 26-Oct-16

Protein chain

Q9RZA4  (BPHY_DEIRA) -  Bacteriophytochrome from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

Seq: 755 a.a.

Struc: 306 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.2.7.13.3 - histidine kinase.
• Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

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

reference

DOI no: 10.1038/srep35279

Sci Rep 6:35279 (2016)

PubMed id: 27756898

The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography.

P.Edlund, H.Takala, E.Claesson, L.Henry, R.Dods, H.Lehtivuori, M.Panman, K.Pande, T.White, T.Nakane, O.Berntsson, E.Gustavsson, P.Båth, V.Modi, S.Roy-Chowdhury, J.Zook, P.Berntsen, S.Pandey, I.Poudyal, J.Tenboer, C.Kupitz, A.Barty, P.Fromme, J.D.Koralek, T.Tanaka, J.Spence, M.Liang, M.S.Hunter, S.Boutet, E.Nango, K.Moffat, G.Groenhof, J.Ihalainen, E.A.Stojković, M.Schmidt, S.Westenhoff.

ABSTRACT

No abstract given.