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Crystal structure of lamin B1 Ig-like domain from human

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

PDB: 7DTG
Type: protein
Length: 708 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.6
Source: Homo sapiens
Molecule: Lamin-B1
UniProt: P20700
Pockets: 6 · best druggability 0.70

Structure

x-ray diffraction · resolution 3.6 · 1 distinct chain · 3% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, F, E	Lamin-B1	protein	118	3% helix, 50% strand	P20700

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	253	0.70	0.86	52	empty
2	161	0.69	0.89	45	empty
3	149	0.63	0.86	40	empty
4	252	0.50	0.74	35	empty
5	204	0.44	0.73	32	empty

Interfaces

6 interfaces between chains.

C–D · 563 Å² buried · 7 hydrogen bonds · protein-protein
A–E · 556 Å² buried · 6 hydrogen bonds · protein-protein
B–F · 540 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 480 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 309 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7DTG · Crystal structure of lamin B1 ig-like domain from human · 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 A 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 7DTG · PDBe 7DTG · UniProt P20700

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