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Ligands
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FXM 2,2-dimethylpropanoyloxymethyl (2r)-5-(aminocarbonyloxymethyl)-2-[(1r)-1-[[(z)-2-(2-azanyl-1,3-thiazol-4-yl)pent-2-enoyl]amino]-2-oxidanylidene-ethyl]-3,6-dihydro-2h-1,3-thiazine-4-carboxylate
GOL Glycerol
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Code : 2EXB   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with FLOMOX
Release Data : 2006-06-13
Compound :
mol_id molecule chains
1 Penicillin-binding protein 4 A
ec: 3.4.16.4, 3.4.99.-
mutation: D261Y
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli BL21(DE3)  (taxid:469008)
strain: DH5 alpha
gene: dacb
expression_system_strain: BL21(DE3)
expression_system_vector_type: PLASMID
expression_system_plasmid: pET21b
Authors : Kishida, H., Unzai, S., Roper, D.I., Lloyd, A., Park, S.-Y., Tame, J.R.H.
Keywords : penicillin-binding protein, penicillin, cephem, penem, FLOMOX, D-alanyl-D-alanine-carboxypeptidase, D-alanyl-D-alanine-endopeptidase, hydrolase
Exp. method : X-RAY DIFFRACTION ( 1.75 Å )
Citation :

Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics

Kishida, H.,Unzai, S.,Roper, D.I.  et al.
(2006)  Biochemistry  45 : 783 - 792

PubMed: 16411754
DOI: 10.1021/bi051533t

Chain : A
UniProt : P24228 (DACB_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. 3.4.16.4 -
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