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Ligands
Code Name Style Show Link
NI Nickel (II) ion
Non-standard Residues
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Glycosylation
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Code : 1BS6   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER
Release Data : 1999-08-27
Compound :
mol_id molecule chains synonym
1 PROTEIN (PEPTIDE DEFORMYLASE) A,B,C PDF
ec: 3.5.1.31
other_details: PDF PROTEIN FORM ESCHERICHIA COLI IS CRYSTALLIZED AS NI2+ CONTAINING FORM, COCRYSTALLIZED WITH PRODUCT PEPTIDE MET-ALA-SER (MAS)
mol_id molecule chains
2 PROTEIN (MET-ALA-SER) D,E,F
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
strain: JM109
cellular_location: CYTOPLASMA
gene: DEF
expression_system_strain: JM109
expression_system_vector_type: PLASMID
expression_system_vector: PKK223-3 (PHARMACIA)
expression_system_plasmid: P925C
expression_system_gene: DEF
mol_id organism_scientific
2
synthetic: yes
other_details: THE PROTEIN WAS CHEMICALLY SYNTHESIZED
Authors : Becker, A., Schlichting, I., Kabsch, W., Groche, D., Schultz, S., Wagner, A.F.V.
Keywords : HYDROLASE, IRON METALLOPROTEASE; PROTEIN SYNTHESIS
Exp. method : X-RAY DIFFRACTION ( 2.10 Å )
Citation :

Iron center, substrate recognition and mechanism of peptide deformylase.

Becker, A.,Schlichting, I.,Kabsch, W.  et al.
(1998)  Nat.Struct.Biol.  5 : 1053 - 1058

PubMed: 9846875
DOI: 10.1038/4162

Structure of Peptide Deformylase and Identification of the Substrate Binding Site

Becker, A.,Schlichting, I.,Kabsch, W.  et al.
(1998)  J.Biol.Chem.  273 : 11413

Isolation and Crystallization of Functionally Competent Escherichia Coli Peptide Deformylase Forms Containing Either Iron or Nickel in the Active Site

Groche, D.,Becker, A.,Schlichting, I.  et al.
(1998)  Biochem.Biophys.Res.Commun.  246 : 342

Chain : A, B, C
UniProt : P0A6K3 (DEF_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N- terminal L-methionyl-[peptide] 3.5.1.88 PubMed:7896716
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