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NMR structure of the DNA-binding domain of cell cycle protein, MBP1(2- 124) from saccharomyces cerevisiae

Analyse NMR structure of the DNA-binding domain of cell cycle protein, MBP1(2- 124)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1L3G
Type: protein
Length: 123 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription factor MBP1
UniProt: P39678
Pockets: 1 · best druggability 0.43

Structure

solution nmr · 1 distinct chain · 29% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription factor MBP1	protein	123	29% helix, 20% strand	P39678

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	60	0.43	0.81	16	empty

Compared structures

1L3G · NMR Structure of the DNA-binding Domain of Cell Cycle Protein, Mbp1(2-124) from… · the same entry in another collection · chain A against A, TM-score 1.00
P39678 · AlphaFold monomer V2.0 prediction for transcription factor MBP1 (P39678) · a predicted model of the same protein · chain A against A, TM-score 0.69

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 P39678
Elsewhere: RCSB PDB 1L3G · PDBe 1L3G · UniProt P39678

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