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The virulence-associated protein hsva from the fire blight pathogen erwinia amylovora is a polyamine amidinotransferase

Analyse The virulence-associated protein hsva from the fire blight pathogen erwinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WPI
Type: protein
Length: 728 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hsva
UniProt: Q58PW8
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hsva	protein	364	26% helix, 22% strand	Q58PW8

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	77	0.76	0.99	34	empty
2	231	0.69	0.86	39	empty
3	211	0.62	0.82	39	empty
4	87	0.51	0.84	29	empty
5	236	0.51	0.76	43	EDO

Interfaces

1 interface between chains.

A–B · 2934 Å² buried · 51 hydrogen bonds · protein-protein

Compared structures

5WPI · The virulence-associated protein HsvA from the fire blight pathogen Erwinia amylovora is… · 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 Q58PW8
Elsewhere: RCSB PDB 5WPI · PDBe 5WPI · UniProt Q58PW8

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