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The crystal structure of the TRP repressor binding protein wrba from pseudomonas aeruginosa

Analyse The crystal structure of the TRP repressor binding protein wrba from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2A5L
Type: protein
Length: 346 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRP repressor binding protein wrba
Ligands: MG
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRP repressor binding protein wrba	protein	171	41% helix, 21% strand	—
B	TRP repressor binding protein wrba	protein	175	39% helix, 21% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	207	0.54	0.78	29	empty
2	56	0.49	0.86	17	empty
3	148	0.47	0.77	24	empty

Interfaces

1 interface between chains.

A–B · 1297 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2A5L · The crystal structure of the Trp repressor binding protein WrbA from Pseudomonas… · 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
Elsewhere: RCSB PDB 2A5L · PDBe 2A5L

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