MolNFT v1 · #188835 · protein

Lxg-associated alpha-helical protein D2 (LAPD2)

7UH4: “Lxg-associated alpha-helical protein D2 (LAPD2)”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.59). MolNFT v1 #188835 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7UH4
Type: protein
Length: 439 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lxg-associated alpha-helical protein D2
Ligands: SO4
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 94% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Lxg-associated alpha-helical protein D2	protein	110	93% helix, 1% strand	—
B	Lxg-associated alpha-helical protein D2	protein	109	93% helix, 1% strand	—
D	Lxg-associated alpha-helical protein D2	protein	110	95% helix, 1% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D

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

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	95	0.59	0.87	16	empty
2	122	0.50	0.80	19	empty

Interfaces

2 interfaces between chains.

A–B · 877 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 844 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7UH4 · LXG-associated alpha-helical protein D2 (LapD2) · 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
Elsewhere: RCSB PDB 7UH4 · PDBe 7UH4

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