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M4L/Y(27D)D/Q89D/T94H mutant of len

Analyse M4L/Y(27D)D/Q89D/T94H mutant of len in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EEU
Type: protein
Length: 225 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kappa-4 immunoglobulin (light chain)
UniProt: P01625
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kappa-4 immunoglobulin (light chain)	protein	112	3% helix, 50% strand	P01625
B	Kappa-4 immunoglobulin (light chain)	protein	113	3% helix, 51% strand	P01625

Ligands and binding sites

IPA · Isopropyl alcohol · additive · 2 copies · chains A, B

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

Pockets

4 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	182	0.62	0.82	23	IPA
2	131	0.39	0.74	25	empty
3	67	0.30	0.74	19	empty
4	65	0.28	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 696 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1EEU · M4L/Y(27D)D/Q89D/T94H mutant of LEN · 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 P01625
Elsewhere: RCSB PDB 1EEU · PDBe 1EEU · UniProt P01625

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