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Solution structure of the thap zinc finger of THAP1 in complex with its DNA target

Analyse Solution structure of the thap zinc finger of THAP1 in complex with its DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KO0
Type: protein + DNA
Length: 119 residues
Chains: 3
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thap domain-containing protein 1; RRM1; Zinc ion
UniProt: Q9NVV9
Ligands: ZN

Structure

solution nmr · 3 distinct chains · 18% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thap domain-containing protein 1	protein	87	18% helix, 7% strand	Q9NVV9
B	RRM1	dna	16	—	—
C	Zinc ion	dna	16	—	—

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Interfaces

3 interfaces between chains.

B–C · 791 Å² buried · 83 hydrogen bonds · nucleic-nucleic
A–B · 606 Å² buried · 13 hydrogen bonds · protein-nucleic
A–C · 543 Å² buried · 11 hydrogen bonds · protein-nucleic

Compared structures

2KO0 · Solution structure of the THAP zinc finger of THAP1 in complex with its DNA target · the same entry in another collection · chain A against A, TM-score 1.00
Q9NVV9 · AlphaFold monomer V2.0 prediction for thap domain-containing protein 1 (Q9NVV9) · a predicted model of the same protein · chain A against A, TM-score 0.67

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 Q9NVV9
Elsewhere: RCSB PDB 2KO0 · PDBe 2KO0 · UniProt Q9NVV9

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