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ABC protein artp in complex with ADP/MG2+

Analyse ABC protein artp in complex with ADP/MG2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OLJ
Type: protein
Length: 484 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amino acid ABC transporter
EC: 3.6.3.21
Ligands: ADP, MG
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Amino acid ABC transporter (EC 3.6.3.21)	protein	242	39% helix, 25% strand	—

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

5 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	758	0.77	0.81	55	empty
2	225	0.67	0.84	24	empty
3	104	0.44	0.78	18	GOL
4	108	0.43	0.78	23	MG, ADP
5	149	0.43	0.75	28	MG, ADP

Interfaces

1 interface between chains.

A–B · 901 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2OLJ · ABC Protein ArtP in complex with ADP/Mg2+ · 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
Elsewhere: RCSB PDB 2OLJ · PDBe 2OLJ

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