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Crystal structure of human lamin-B1 coil 2 segment

Analyse Crystal structure of human lamin-B1 coil 2 segment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TYY
Type: protein
Length: 146 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lamin-B1
UniProt: P20700

Structure

x-ray diffraction · 2 distinct chains · 92% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lamin-B1	protein	75	89% helix, 0% strand	P20700
B	Lamin-B1	protein	71	94% helix, 0% strand	P20700

Interfaces

1 interface between chains.

A–B · 2002 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3TYY · Crystal Structure of Human Lamin-B1 Coil 2 Segment · the same entry in another collection · chain A against A, TM-score 1.00
P20700 · AlphaFold monomer V2.0 prediction for lamin-B1 (P20700) · a predicted model of the same protein · chain B against A, TM-score 0.93

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 P20700
Elsewhere: RCSB PDB 3TYY · PDBe 3TYY · UniProt P20700

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