MolNFT v1 · #68238 · protein

Lasr-TP4 complex

3JPU · Transcriptional activator protein lasr: “Lasr-TP4 complex”. X-ray diffraction, 1 ligand (TY4), 10 pockets (best druggability 0.83). MolNFT v1 #68238 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3JPU
Type: protein
Length: 808 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional activator protein lasr
UniProt: P25084
Ligands: TY4
Pockets: 10 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, E	Transcriptional activator protein lasr	protein	161	52% helix, 17% strand	P25084
C	Transcriptional activator protein lasr	protein	163	50% helix, 17% strand	P25084
D	Transcriptional activator protein lasr	protein	162	51% helix, 17% strand	P25084

Ligands and binding sites

TY4 · 4-bromo-2-({[(2-chlorophenyl)carbonyl]amino}methyl)-6-methylphenyl 2,4-dichlorobenzoate · ligand · 5 copies · chains A, B, C, D, E

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

Pockets

10 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	209	0.83	0.96	30	TY4
2	190	0.81	0.95	29	TY4
3	218	0.81	0.94	30	TY4
4	242	0.81	0.93	31	TY4
5	207	0.80	0.94	33	TY4

Interfaces

6 interfaces between chains.

B–C · 949 Å² buried · 9 hydrogen bonds · protein-protein
D–E · 935 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 182 Å² buried · 1 hydrogen bond · protein-protein
A–B · 144 Å² buried · 1 hydrogen bond · protein-protein
B–E · 84 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3JPU · LasR-TP4 complex · the same entry in another collection · chain E against E, TM-score 1.00
P25084 · AlphaFold monomer V2.0 prediction for transcriptional activator protein lasr (P25084) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 P25084
Elsewhere: RCSB PDB 3JPU · PDBe 3JPU · UniProt P25084

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