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Formyl-met-ala-ser bound crystal structure of class II peptide deformylase from methicillin resistant staphylococcus aureus

Analyse Formyl-met-ala-ser bound crystal structure of class II peptide deformylase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JFO
Type: protein
Length: 186 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide deformylase; Fme-ala-ser
EC: 3.5.1.88
UniProt: P68826
Ligands: MG

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptide deformylase (EC 3.5.1.88)	protein	183	28% helix, 25% strand	P68826
B	Fme-ala-ser	protein	3	0% helix, 33% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 330 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (formylation, oxidation).

Compared structures

6JFO · Formyl-Met-Ala-Ser bound crystal structure of class II peptide deformylase from… · the same entry in another collection · chain A against A, TM-score 1.00
P68826 · AlphaFold monomer V2.0 prediction for peptide deformylase (P68826) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P68826
Elsewhere: RCSB PDB 6JFO · PDBe 6JFO · UniProt P68826

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