Research workbench

LMO4-LIM2 in complex with DEAF1 (404-418)

Analyse LMO4-LIM2 in complex with DEAF1 (404-418) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MBV
Type: protein
Length: 96 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fusion protein of lim domain transcription factor LMO4 (77- 147) and DEAF1 (404-418)
UniProt: P61969, Q9Z1T5
Ligands: ZN

Structure

solution nmr · 1 distinct chain · 0% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fusion protein of lim domain transcription factor LMO4 (77- 147) and DEAF1 (404-418)	protein	96	0% helix, 23% strand	P61969, Q9Z1T5

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Compared structures

2MBV · LMO4-LIM2 in complex with DEAF1 (404-418) · the same entry in another collection · chain A against A, TM-score 1.00
P61969 · AlphaFold monomer V2.0 prediction for lim domain transcription factor LMO4 (P61969) · a predicted model of the same protein · chain A against A, TM-score 0.62
Q9Z1T5 · AlphaFold monomer V2.0 prediction for deformed epidermal autoregulatory factor 1 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.27

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 P61969
Every structure of UniProt Q9Z1T5
Elsewhere: RCSB PDB 2MBV · PDBe 2MBV · UniProt P61969 · UniProt Q9Z1T5

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