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A novel ADP- and zinc-binding fold from function-directed in vitro evolution

Analyse A novel ADP- and zinc-binding fold from function-directed in vitro evolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UW1
Type: protein
Length: 67 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Artificial nucleotide binding protein (anbp)
Ligands: ADP, ZN
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Artificial nucleotide binding protein (anbp)	protein	67	31% helix, 24% strand	—

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
ZN · Zinc 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	65	0.31	0.74	9	empty

Compared structures

1UW1 · A Novel ADP- and Zinc-binding fold from function-directed in vitro evolution · 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 1UW1 · PDBe 1UW1

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