MolNFT v1 · #114542 · protein

Crystal structure of 4-COUMARATE:COA ligase complexed with adenosine monophosphate and coenzyme a

5BSR · 4-coumarate--CoA ligase 2: “Crystal structure of 4-COUMARATE:COA ligase complexed with adenosine monophosphate and coenzyme a”. X-ray diffraction, 2 ligands (COA, AMP), 2 pockets (best druggability 0.83). MolNFT v1 #114542 on…

PDB: 5BSR
Type: protein
Length: 528 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-coumarate--CoA ligase 2
EC: 6.2.1.12
UniProt: O24146
Ligands: COA, AMP
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-coumarate--CoA ligase 2 (EC 6.2.1.12)	protein	528	32% helix, 24% strand	O24146

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
AMP · Adenosine monophosphate · ligand · chains A
GOL · Glycerol · additive · 4 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	1136	0.83	0.84	124	COA, AMP, GOL
2	68	0.30	0.74	13	empty

Compared structures

O24146 · AlphaFold monomer V2.0 prediction for 4-coumarate--CoA ligase 2 (O24146) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 O24146
Elsewhere: RCSB PDB 5BSR · PDBe 5BSR · UniProt O24146

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