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Crystal structure of a putative lipoate-protein ligase a (SP_1160) from streptococcus pneumoniae TIGR4 at 1.99 a resolution

Analyse Crystal structure of a putative lipoate-protein ligase a (SP_1160) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VQZ
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipoate-protein ligase, putative
UniProt: Q97QP1
Ligands: UNL
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipoate-protein ligase, putative	protein	330	32% helix, 28% strand	Q97QP1

Ligands and binding sites

UNL · Unknown ligand · ligand · chains A
EDO · 1,2-ethanediol · additive · 17 copies · chains A

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

Pockets

2 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	431	0.62	0.77	56	EDO
2	132	0.42	0.76	26	EDO

Modifications

Observed in the structure: 4 modified, 1 covalent (engineered, covalent ligand).

Compared structures

1VQZ · Crystal structure of a putative lipoate-protein ligase a (sp_1160) from streptococcus… · 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 Q97QP1
Elsewhere: RCSB PDB 1VQZ · PDBe 1VQZ · UniProt Q97QP1

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