MolNFT v1 · #175468 · protein

The functional characterization and crystal structure of the bifunctional thioesterase catalyzing epimerization and cyclization

7CRN · Non-ribosomal peptide synthetase 4: “The functional characterization and crystal structure of the bifunctional thioesterase catalyzing…”. X-ray diffraction, 5 pockets (best druggability 0.73). MolNFT v1 #175468 on GenesisL1: 3D…

PDB: 7CRN
Type: protein
Length: 791 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-ribosomal peptide synthetase 4
UniProt: A0A1J0R317
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Non-ribosomal peptide synthetase 4	protein	264	42% helix, 15% strand	A0A1J0R317
C	Non-ribosomal peptide synthetase 4	protein	263	43% helix, 15% strand	A0A1J0R317

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	559	0.73	0.81	87	empty
2	104	0.59	0.87	28	empty
3	179	0.53	0.79	40	empty
4	110	0.49	0.80	26	empty
5	65	0.34	0.77	16	empty

Interfaces

2 interfaces between chains.

B–C · 1076 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 978 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7CRN · The Functional Characterization and Crystal Structure of the Bifunctional Thioesterase… · the same entry in another collection · chain A against A, 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 7CRN · PDBe 7CRN · UniProt A0A1J0R317

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