MolNFT v1 · #63821 · protein

Rifr - type II thioesterase from rifamycin NRPS/PKS biosynthetic pathway - form 1

3FLA: “Rifr - type II thioesterase from rifamycin NRPS/PKS biosynthetic pathway - form 1”. X-ray diffraction, 1 ligand (CL), 8 pockets (best druggability 0.77). MolNFT v1 #63821 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3FLA
Type: protein
Length: 492 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rifr
EC: 3.1.2.-
UniProt: Q7BUF9
Ligands: CL
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Rifr (EC 3.1.2.-)	protein	246	44% helix, 16% strand	Q7BUF9

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.77	0.97	24	CL
2	109	0.76	0.96	22	CL
3	107	0.57	0.84	22	empty
4	115	0.54	0.82	20	empty
5	105	0.53	0.83	20	empty

Interfaces

1 interface between chains.

A–B · 490 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

3FLA · RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 1 · 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 Q7BUF9
Elsewhere: RCSB PDB 3FLA · PDBe 3FLA · UniProt Q7BUF9

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