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Crystal structure of the di-domain ARO/CYC stfq from the steffimycin biosynthetic pathway

Analyse Crystal structure of the di-domain ARO/CYC stfq from the steffimycin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XRT
Type: protein
Length: 601 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Stfq AROMATASE/CYCLASE
UniProt: Q2PA00
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Stfq AROMATASE/CYCLASE	protein	302	31% helix, 47% strand	Q2PA00
B	Stfq AROMATASE/CYCLASE	protein	299	32% helix, 45% strand	Q2PA00

Ligands and binding sites

FMT · Formic acid · additive · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1124	0.82	0.83	139	FMT
2	390	0.71	0.82	37	empty
3	99	0.41	0.77	24	empty
4	83	0.35	0.75	12	empty
5	50	0.35	0.79	13	empty

Interfaces

1 interface between chains.

A–B · 645 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4XRT · Crystal structure of the di-domain ARO/CYC StfQ from the steffimycin biosynthetic pathway · 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 Q2PA00
Elsewhere: RCSB PDB 4XRT · PDBe 4XRT · UniProt Q2PA00

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