PDBsum entry 3q15

Hydrolase/kinase

PDB id: 3q15

Contents

Protein chains

365 a.a. *

332 a.a. *

116 a.a. *

100 a.a. *

Ligands

GOL ×2

SO4 ×2

Metals

_MG ×2

Waters ×236

* Residue conservation analysis

PDB id:

3q15

Name:

Hydrolase/kinase

Title:

Crystal structure of raph complexed with spo0f

Structure:

Response regulator aspartate phosphatase h. Chain: a, b. Synonym: psp28. Engineered: yes. Sporulation initiation phosphotransferase f. Chain: c, d. Synonym: stage 0 sporulation protein f. Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Gene: bsu06830, raph, yeeh, yzqa. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: bsu37130, spo0f.

Resolution:

2.19Å R-factor: 0.223 R-free: 0.268

Authors:

V.Parashar,M.B.Neiditch

Key ref:

V.Parashar et al. (2011). Structural basis of response regulator dephosphorylation by Rap phosphatases. Plos Biol, 9, e1000589. PubMed id: 21346797

Date:

16-Dec-10 Release date: 23-Feb-11

Protein chain

Q59HN8  (RAPH_BACSU) -  Response regulator aspartate phosphatase H from Bacillus subtilis (strain 168)

Seq: 376 a.a.

Struc: 365 a.a.

Protein chain

Q59HN8  (RAPH_BACSU) -  Response regulator aspartate phosphatase H from Bacillus subtilis (strain 168)

Seq: 376 a.a.

Struc: 332 a.a.

Protein chain

P06628  (SP0F_BACSU) -  Sporulation initiation phosphotransferase F from Bacillus subtilis (strain 168)

Seq: 124 a.a.

Struc: 116 a.a.

Protein chain

P06628  (SP0F_BACSU) -  Sporulation initiation phosphotransferase F from Bacillus subtilis (strain 168)

Seq: 124 a.a.

Struc: 100 a.a.

Enzyme reactions

• Enzyme class 2: Chains A, B: E.C.3.1.3.- - ?????
• Enzyme class 3: Chains C, D: E.C.2.7.-.-

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.

Plos Biol 9:e1000589 (2011)

PubMed id: 21346797

Structural basis of response regulator dephosphorylation by Rap phosphatases.

V.Parashar, N.Mirouze, D.A.Dubnau, M.B.Neiditch.

ABSTRACT

No abstract given.