MolNFT v1 · #148466 · protein

Tryptophan repressor trpr from E.COLI with 3-indolepropionic acid

6F7F · TRP operon repressor: “Tryptophan repressor trpr from E.COLI with 3-indolepropionic acid”. X-ray diffraction, 1 ligand (IOP), 7 pockets (best druggability 0.62). MolNFT v1 #148466 on GenesisL1: 3D structure, binding sites and…

PDB: 6F7F
Type: protein
Length: 408 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRP operon repressor
UniProt: P0A881
Ligands: IOP
Pockets: 7 · best druggability 0.62

Structure

x-ray diffraction · 4 distinct chains · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	TRP operon repressor	protein	102	81% helix, 0% strand	P0A881
A	TRP operon repressor	protein	102	80% helix, 0% strand	P0A881
D	TRP operon repressor	protein	103	78% helix, 0% strand	P0A881
C	TRP operon repressor	protein	101	79% helix, 0% strand	P0A881

Ligands and binding sites

IOP · Indolylpropionic acid · ligand · 4 copies · chains B, A, D, C

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

Pockets

7 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	355	0.62	0.78	41	empty
2	220	0.55	0.78	24	empty
3	83	0.47	0.82	17	IOP
4	86	0.43	0.79	16	IOP
5	64	0.42	0.82	14	IOP

Interfaces

6 interfaces between chains.

D–C · 2358 Å² buried · 22 hydrogen bonds · protein-protein
B–A · 2330 Å² buried · 21 hydrogen bonds · protein-protein
B–C · 302 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 251 Å² buried · 1 hydrogen bond · protein-protein
A–D · 176 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6F7F · Tryptophan Repressor TrpR from E.coli with 3-Indolepropionic acid · the same entry in another collection · chain C against C, TM-score 1.00
P0A881 · AlphaFold monomer V2.0 prediction for TRP operon repressor (P0A881) · a predicted model of the same protein · chain C against A, TM-score 0.97

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 P0A881
Elsewhere: RCSB PDB 6F7F · PDBe 6F7F · UniProt P0A881

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