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Mouse laminin ALPHA1 chain, domains LG4-5

Analyse Mouse laminin ALPHA1 chain, domains LG4-5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JD4
Type: protein
Length: 750 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Laminin subunit alpha-1
UniProt: P19137
Ligands: MG, CL
Pockets: 5 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Laminin subunit alpha-1	protein	375	2% helix, 49% strand	P19137
B	Laminin subunit alpha-1	protein	375	1% helix, 51% strand	P19137

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A, B
CL · Chloride ion · ion · 3 copies · chains A, B

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

Pockets

5 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	230	0.59	0.80	36	empty
2	204	0.59	0.81	32	empty
3	252	0.55	0.77	35	CL
4	111	0.44	0.78	19	empty
5	61	0.30	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 454 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

2JD4 · Mouse laminin alpha1 chain, domains LG4-5 · the same entry in another collection · chain A against A, TM-score 1.00

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 P19137
Elsewhere: RCSB PDB 2JD4 · PDBe 2JD4 · UniProt P19137

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