PDBsum entry 3mfd

Hydrolase

PDB id: 3mfd

Contents

Protein chains

326 a.a. *

306 a.a. *

Ligands

CIT ×4

EDO ×8

Waters ×773

* Residue conservation analysis

PDB id:

3mfd

Name:

Hydrolase

Title:

The structure of the beta-lactamase superfamily domain of d-alanyl-d- alanine carboxypeptidase from bacillus subtilis

Structure:

D-alanyl-d-alanine carboxypeptidase dacb. Chain: a, b. Fragment: beta-lactamase domain residues 27-358. Synonym: dd-carboxypeptidase, dd-peptidase, penicillin-binding protein 5 , Pbp-5 . Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Strain: 168. Gene: bsu23190, dacb, dacc. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.75Å R-factor: 0.166 R-free: 0.190

Authors:

M.E.Cuff,E.Rakowski,K.Buck,A.Joachimiak,Midwest Center For Structural Genomics (Mcsg)

Key ref:

M.E.Cuff et al. The structure of the beta-Lactamase superfamily domai d-Alanyl-D-Alanine carboxypeptidase from bacillus sub. To be published, .

Date:

01-Apr-10 Release date: 19-May-10

Protein chain

P35150  (DACB_BACSU) -  D-alanyl-D-alanine carboxypeptidase DacB from Bacillus subtilis (strain 168)

Seq: 382 a.a.

Struc: 326 a.a.

Protein chain

P35150  (DACB_BACSU) -  D-alanyl-D-alanine carboxypeptidase DacB from Bacillus subtilis (strain 168)

Seq: 382 a.a.

Struc: 306 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase.
• Reaction: D-alanyl-D-alanine + H₂O = 2 D-alanine

+ = 2 × (Bound ligand (Het Group name = EDO) matches with 42.00% similarity)

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