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KSQ+AT from first module of the pikromycin synthase

Analyse KSQ+AT from first module of the pikromycin synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7UWR
Type: protein
Length: 1,674 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NARBONOLIDE/10-deoxymethynolide synthase PIKA1, modules 1 and 2
EC: 2.3.1.239, 2.3.1.240
UniProt: Q9ZGI5
Pockets: 14 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	NARBONOLIDE/10-deoxymethynolide synthase PIKA1, modules 1 and 2 (EC 2.3.1.239, 2.3.1.240)	protein	837	40% helix, 20% strand	Q9ZGI5

Pockets

14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	171	0.82	0.97	37	empty
2	217	0.71	0.87	35	empty
3	216	0.69	0.86	37	empty
4	313	0.64	0.80	47	empty
5	313	0.64	0.80	47	empty

Interfaces

1 interface between chains.

A–B · 2784 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

7UWR · KSQ+AT from first module of the pikromycin synthase · 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 Q9ZGI5
Elsewhere: RCSB PDB 7UWR · PDBe 7UWR · UniProt Q9ZGI5

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