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Crystal structure of lamin a COIL1B tetramer

Analyse Crystal structure of lamin a COIL1B tetramer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SNZ
Type: protein
Length: 604 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prelamin-A/C
UniProt: P02545
Pockets: 6 · best druggability 0.51

Structure

x-ray diffraction · 4 distinct chains · 98% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prelamin-A/C	protein	160	97% helix, 0% strand	P02545
B	Prelamin-A/C	protein	155	98% helix, 0% strand	P02545
C	Prelamin-A/C	protein	146	99% helix, 0% strand	P02545
D	Prelamin-A/C	protein	143	97% helix, 0% strand	P02545

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	261	0.51	0.75	35	empty
2	195	0.47	0.75	16	empty
3	152	0.40	0.73	14	empty
4	96	0.38	0.76	16	empty
5	97	0.35	0.74	17	empty

Interfaces

6 interfaces between chains.

A–B · 4347 Å² buried · 28 hydrogen bonds · protein-protein
C–D · 4099 Å² buried · 26 hydrogen bonds · protein-protein
B–C · 531 Å² buried · 5 hydrogen bonds · protein-protein
B–D · 312 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 121 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6SNZ · Crystal structure of lamin A coil1b tetramer · the same entry in another collection · chain D against D, TM-score 1.00
P02545 · AlphaFold monomer V2.0 prediction for prelamin-A/C (P02545) · a predicted model of the same protein · chain D 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 P02545
Elsewhere: RCSB PDB 6SNZ · PDBe 6SNZ · UniProt P02545

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