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The macro domain is an ADP-ribose binding module

Analyse The macro domain is an ADP-ribose binding module in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BFR
Type: protein
Length: 192 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein AF1521
UniProt: O28751
Ligands: ADP, MG
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein AF1521	protein	192	44% helix, 21% strand	O28751

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	221	0.58	0.79	30	ADP

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, formylation).

Compared structures

2BFR · The Macro domain is an ADP-ribose binding module · the same entry in another collection · chain A against A, TM-score 1.00
O28751 · AlphaFold monomer V2.0 prediction for ADP-ribose glycohydrolase AF_1521 (O28751) · a predicted model of the same protein · 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 O28751
Elsewhere: RCSB PDB 2BFR · PDBe 2BFR · UniProt O28751

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