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Crystal structure of a nonribosomal peptide synthetase heterocyclization domain.

Analyse Crystal structure of a nonribosomal peptide synthetase heterocyclization domain. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T3E
Type: protein
Length: 862 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bacillamide synthetase heterocyclization domain
UniProt: A0A0N0Y601
Ligands: SO4
Pockets: 10 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bacillamide synthetase heterocyclization domain	protein	432	40% helix, 22% strand	A0A0N0Y601
B	Bacillamide synthetase heterocyclization domain	protein	430	40% helix, 22% strand	A0A0N0Y601

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	464	0.84	0.90	59	empty
2	438	0.81	0.88	59	empty
3	693	0.78	0.83	72	empty
4	214	0.65	0.84	33	empty
5	74	0.36	0.77	16	empty

Interfaces

1 interface between chains.

A–B · 1114 Å² buried · 16 hydrogen bonds · protein-protein

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 A0A0N0Y601
Elsewhere: RCSB PDB 5T3E · PDBe 5T3E · UniProt A0A0N0Y601

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