MolNFT v1 · #49316 · protein

Crystal structure of tandem ZPR1 domains

2QKD · Zinc finger protein ZPR1: “Crystal structure of tandem ZPR1 domains”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.41). MolNFT v1 #49316 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2QKD
Type: protein
Length: 384 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Zinc finger protein ZPR1
UniProt: Q62384
Ligands: ZN
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zinc finger protein ZPR1	protein	384	23% helix, 35% strand	Q62384

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
FMT · Formic acid · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	133	0.41	0.74	22	empty
2	96	0.38	0.76	19	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2QKD · Crystal structure of tandem ZPR1 domains · the same entry in another collection · chain A against A, TM-score 1.00
Q62384 · AlphaFold monomer V2.0 prediction for zinc finger protein ZPR1 (Q62384) · a predicted model of the same protein · chain A against A, TM-score 0.43

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 Q62384
Elsewhere: RCSB PDB 2QKD · PDBe 2QKD · UniProt Q62384

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