MolNFT v1 · #155560 · protein

Crystal structure of FEM1B

6LBF · Protein fem-1 homolog B: “Crystal structure of FEM1B”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.68). MolNFT v1 #155560 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6LBF
Type: protein
Length: 685 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein fem-1 homolog B
UniProt: Q9UK73
Ligands: SO4
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein fem-1 homolog B	protein	343	52% helix, 5% strand	Q9UK73
B	Protein fem-1 homolog B	protein	342	51% helix, 5% strand	Q9UK73

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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	631	0.68	0.76	61	empty
2	440	0.65	0.78	46	empty

Interfaces

1 interface between chains.

A–B · 960 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6LBF · Crystal structure of FEM1B · the same entry in another collection · chain A against A, TM-score 1.00
Q9UK73 · AlphaFold monomer V2.0 prediction for protein fem-1 homolog B (Q9UK73) · a predicted model of the same protein · chain B 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 Q9UK73
Elsewhere: RCSB PDB 6LBF · PDBe 6LBF · UniProt Q9UK73

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