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Crystal structure of trmo from pseudomonas aeruginosa

Analyse Crystal structure of trmo from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BU1
Type: protein
Length: 415 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative tRNA (ADENINE(37)-N6)-methyltransferase
UniProt: A0A080VNW8
Ligands: SAM
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative tRNA (ADENINE(37)-N6)-methyltransferase	protein	205	21% helix, 36% strand	A0A080VNW8
B	Putative tRNA (ADENINE(37)-N6)-methyltransferase	protein	210	20% helix, 36% strand	A0A080VNW8

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B

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

Pockets

2 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	437	0.68	0.79	52	SAM
2	306	0.62	0.79	42	SAM

Interfaces

1 interface between chains.

A–B · 2913 Å² buried · 59 hydrogen bonds · protein-protein

Compared structures

7BU1 · Crystal structure of TrmO from Pseudomonas aeruginosa · 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 A0A080VNW8
Elsewhere: RCSB PDB 7BU1 · PDBe 7BU1 · UniProt A0A080VNW8

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