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Crystal structure of the bacterial dehalococcoides mccartyi ELP3 with desulfo-CoA

Analyse Crystal structure of the bacterial dehalococcoides mccartyi ELP3 with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IA6
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ELP3 family, ELP3 family
UniProt: A0A1C7D1B7
Ligands: DCA, FES, PO4
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ELP3 family, ELP3 family	protein	388	34% helix, 24% strand	A0A1C7D1B7

Ligands and binding sites

DCA · Desulfo-coenzyme A · ligand · chains A
FES · Fe2/s2 (inorganic) cluster · ligand · chains A
PO4 · Phosphate ion · ion · 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	775	0.74	0.79	79	DCA, PO4
2	245	0.54	0.77	33	empty

Compared structures

6IA6 · Crystal structure of the bacterial Dehalococcoides mccartyi Elp3 with desulfo-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 A0A1C7D1B7
Elsewhere: RCSB PDB 6IA6 · PDBe 6IA6 · UniProt A0A1C7D1B7

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