MolNFT v1 · #156773 · protein

Rfxank ankyrin repeats in complex with a RFX7 peptide

6MEW · DNA-binding protein rfxank: “Rfxank ankyrin repeats in complex with a RFX7 peptide”. X-ray diffraction, 1 ligand (UNX), 3 pockets (best druggability 0.79). MolNFT v1 #156773 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6MEW
Type: protein
Length: 353 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA-binding protein rfxank; RFX7 peptide
UniProt: O14593
Ligands: UNX
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 44% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	DNA-binding protein rfxank	protein	162	52% helix, 0% strand	O14593
B	RFX7 peptide	protein	13	0% helix, 0% strand	—
D	RFX7 peptide	protein	16	0% helix, 0% strand	—

Ligands and binding sites

UNX · Unknown atom or ion · ion · 53 copies · chains A, C, B, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	147	0.79	0.96	25	UNX
2	73	0.39	0.78	15	UNX
3	82	0.38	0.77	15	UNX

Interfaces

6 interfaces between chains.

C–D · 851 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 810 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 473 Å² buried · 9 hydrogen bonds · protein-protein
B–D · 338 Å² buried · 8 hydrogen bonds · protein-protein
A–D · 164 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6MEW · RFXANK ankyrin repeats in complex with a RFX7 peptide · the same entry in another collection · chain A against A, TM-score 1.00
O14593 · AlphaFold monomer V2.0 prediction for DNA-binding protein rfxank (O14593) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O14593
Elsewhere: RCSB PDB 6MEW · PDBe 6MEW · UniProt O14593

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