MolNFT v1 · #182566 · protein

Structure of de novo designed beta sheet heterodimer LHD101A53/B4

7MWR · LHD101A54: “Structure of de novo designed beta sheet heterodimer LHD101A53/B4”. X-ray diffraction, 4 pockets (best druggability 0.74). MolNFT v1 #182566 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7MWR
Type: protein
Length: 453 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LHD101A54; LHD101B4
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LHD101A54	protein	204	66% helix, 13% strand	—
B	LHD101B4	protein	249	73% helix, 11% strand	—

Ligands and binding sites

MLI · Malonate ion · additive · chains A

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	225	0.74	0.89	23	empty
2	52	0.34	0.78	16	empty
3	53	0.27	0.74	19	empty
4	50	0.26	0.74	11	empty

Interfaces

1 interface between chains.

A–B · 921 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

7MWR · Structure of De Novo designed beta sheet heterodimer LHD101A53/B4 · 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 7MWR · PDBe 7MWR

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