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The binary complex of prnb (the second enzyme in pyrrolnitrin biosynthesis pathway) and cyanide

Analyse The binary complex of prnb (the second enzyme in pyrrolnitrin biosynthesis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X66
Type: protein
Length: 343 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prnb
UniProt: P95481
Ligands: HEM, CYN, SO4
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prnb	protein	343	70% helix, 2% strand	P95481

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CYN · Cyanide ion · ion · chains A
SO4 · Sulfate ion · ion · 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	542	0.79	0.85	49	CYN, HEM

Compared structures

2X66 · The binary complex of PrnB (the second enzyme in pyrrolnitrin biosynthesis pathway) and… · the same entry in another collection · chain A against A, TM-score 1.00
P95481 · AlphaFold monomer V2.0 prediction for monodechloroaminopyrrolnitrin synthase prnb (P95481) · a predicted model of the same protein · 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 P95481
Elsewhere: RCSB PDB 2X66 · PDBe 2X66 · UniProt P95481

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