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Crystal structure of lamin-B1

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

PDB: 3UMN
Type: protein
Length: 352 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lamin-B1
UniProt: P20700
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Lamin-B1	protein	118	0% helix, 52% strand	P20700
B	Lamin-B1	protein	116	0% helix, 51% strand	P20700

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	232	0.68	0.85	53	empty
2	364	0.53	0.73	36	empty

Interfaces

3 interfaces between chains.

B–C · 505 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 51 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 13 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3UMN · Crystal Structure of Lamin-B1 · the same entry in another collection · chain C against C, 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 0.96

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 3UMN · PDBe 3UMN · UniProt P20700

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