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Structure of blmi, a type-II acyl-carrier-protein from streptomyces verticillus involved in bleomycin biosynthesis

Analyse Structure of blmi, a type-II acyl-carrier-protein from streptomyces verticillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NEO
Type
protein
Length
83 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptide synthetase nrps type II-pcp
UniProt
Q9XC48

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptide synthetase nrps type II-pcpprotein8366% helix, 0% strandQ9XC48

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · chains A
  • PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains A

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

Modifications

Observed in the structure: 2 modified (engineered, methylation).

Compared structures

  • 4NEO · Structure of BlmI, a type-II acyl-carrier-protein from Streptomyces verticillus involved… · the same entry in another collection · chain A against A, TM-score 1.00

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