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Pyridine synthase, pbtd, from GE2270 biosynthesis

Analyse Pyridine synthase, pbtd, from GE2270 biosynthesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5W98
Type: protein
Length: 300 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pbtd
UniProt: U5Q3T2
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pbtd	protein	300	63% helix, 7% strand	U5Q3T2

Ligands and binding sites

MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	645	0.70	0.78	50	empty

Compared structures

5W98 · Pyridine synthase, PbtD, from GE2270 biosynthesis · 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 U5Q3T2
Elsewhere: RCSB PDB 5W98 · PDBe 5W98 · UniProt U5Q3T2

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