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NMR structures of the C-terminal globular domain of human lamin A/C

Analyse NMR structures of the C-terminal globular domain of human lamin A/C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IVT
Type: protein
Length: 122 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lamin A/C
UniProt: P02545

Structure

solution nmr · 1 distinct chain · 2% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lamin A/C	protein	122	2% helix, 44% strand	P02545

Compared structures

1IVT · NMR structures of the C-terminal globular domain of human lamin A/C · the same entry in another collection · chain A against A, TM-score 1.00
P02545 · AlphaFold monomer V2.0 prediction for prelamin-A/C (P02545) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 P02545
Elsewhere: RCSB PDB 1IVT · PDBe 1IVT · UniProt P02545

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