MolNFT v1 · #36352 · protein

Crystal structure of the autoinhibitory switch in formin MDIA1; the DID/DAD complex

2F31 · Diaphanous protein homolog 1: “Crystal structure of the autoinhibitory switch in formin MDIA1; the DID/DAD complex”. X-ray diffraction, 2 pockets (best druggability 0.35). MolNFT v1 #36352 on GenesisL1: 3D structure, binding sites…

PDB: 2F31
Type: protein
Length: 248 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diaphanous protein homolog 1
UniProt: O08808
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diaphanous protein homolog 1	protein	228	75% helix, 0% strand	O08808
B	Diaphanous protein homolog 1	protein	20	55% helix, 0% strand	O08808

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	50	0.35	0.80	11	empty
2	57	0.27	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 829 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2F31 · Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex · the same entry in another collection · chain A against A, TM-score 1.00
O08808 · AlphaFold monomer V2.0 prediction for protein diaphanous homolog 1 (O08808) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O08808
Elsewhere: RCSB PDB 2F31 · PDBe 2F31 · UniProt O08808

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