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Crystal structure of vipf from legionella hackeliae in complex with CoA

Analyse Crystal structure of vipf from legionella hackeliae in complex with CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WQC
Type: protein
Length: 293 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-terminal acetyltransferase, gnat family
UniProt: A0A0A8UKD4
Ligands: COA
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-terminal acetyltransferase, gnat family	protein	293	34% helix, 33% strand	A0A0A8UKD4

Ligands and binding sites

COA · Coenzyme A · ligand · 2 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	293	0.69	0.83	31	COA
2	413	0.57	0.74	50	COA

Modifications

Observed in the structure: 8 modified, 1 covalent (engineered, covalent ligand).

Compared structures

6WQC · Crystal structure of VipF from Legionella hackeliae in complex with CoA · 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 A0A0A8UKD4
Elsewhere: RCSB PDB 6WQC · PDBe 6WQC · UniProt A0A0A8UKD4

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