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The mutant of bifunctional thioesterase catalyzing epimerization and cyclization

Analyse The mutant of bifunctional thioesterase catalyzing epimerization and cyclization in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DXO
Type: protein
Length: 792 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-ribosomal peptide synthetase 4
UniProt: A0A1J0R317
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Non-ribosomal peptide synthetase 4	protein	264	41% helix, 16% strand	A0A1J0R317

Pockets

7 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	470	0.70	0.80	61	empty
2	106	0.58	0.85	29	empty
3	107	0.51	0.82	24	empty
4	161	0.51	0.79	31	empty
5	143	0.49	0.79	26	empty

Interfaces

2 interfaces between chains.

B–C · 1090 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 940 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7DXO · The mutant of bifunctional thioesterase catalyzing epimerization and cyclization · the same entry in another collection · chain C against C, TM-score 1.00

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 A0A1J0R317
Elsewhere: RCSB PDB 7DXO · PDBe 7DXO · UniProt A0A1J0R317

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