Research workbench

NMR structure of fusion of ctip (641-685) to LMO4-LIM1 (18-82)

Analyse NMR structure of fusion of ctip (641-685) to LMO4-LIM1 (18-82) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2L4Z
Type: protein
Length: 121 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA endonuclease RBBP8,LIM domain transcription factor LMO4
EC: 3.1.-.-
UniProt: Q99708, P61968
Ligands: ZN

Structure

solution nmr · 1 distinct chain · 11% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA endonuclease RBBP8,LIM domain transcription factor LMO4 (EC 3.1.-.-)	protein	121	11% helix, 17% strand	Q99708, P61968

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

2L4Z · NMR structure of fusion of CtIP (641-685) to LMO4-LIM1 (18-82) · the same entry in another collection · chain A against A, TM-score 1.00
P61968 · AlphaFold monomer V2.0 prediction for lim domain transcription factor LMO4 (P61968) · a predicted model of the same protein · chain A against A, TM-score 0.51
Q99708 · AlphaFold monomer V2.0 prediction for DNA endonuclease RBBP8 (Q99708) · 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 Q99708
Every structure of UniProt P61968
Elsewhere: RCSB PDB 2L4Z · PDBe 2L4Z · UniProt Q99708 · UniProt P61968

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