MolNFT v1 · #152565 · protein

Structural basis of aimp signaling molecule recognition by aimr in spbeta group of bacteriophages

6IM4 · Aimr transcriptional regulator: “Structural basis of aimp signaling molecule recognition by aimr in spbeta group of bacteriophages”. X-ray diffraction, 9 pockets (best druggability 0.67). MolNFT v1 #152565 on GenesisL1: 3D…

PDB: 6IM4
Type: protein
Length: 792 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aimr transcriptional regulator; Gly-met-pro-arg-gly-ala
UniProt: O64094
Pockets: 9 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aimr transcriptional regulator	protein	390	72% helix, 0% strand	O64094
C, D	Gly-met-pro-arg-gly-ala	protein	6	0% helix, 0% strand	—

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	558	0.67	0.77	55	empty
2	426	0.66	0.79	41	empty
3	407	0.64	0.78	40	empty
4	153	0.43	0.75	24	empty
5	89	0.38	0.76	14	empty

Interfaces

3 interfaces between chains.

A–D · 571 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 567 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 245 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6IM4 · Structural basis of AimP signaling molecule recognition by AimR in Spbeta group of… · 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 O64094
Elsewhere: RCSB PDB 6IM4 · PDBe 6IM4 · UniProt O64094

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