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Structure of FEM1C

Analyse Structure of FEM1C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LF0
Type: protein
Length: 773 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein fem-1 homolog C
UniProt: Q96JP0
Ligands: SO4
Pockets: 8 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein fem-1 homolog C	protein	392	57% helix, 3% strand	Q96JP0
B	Protein fem-1 homolog C	protein	381	57% helix, 3% strand	Q96JP0

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A, B

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

Pockets

8 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	963	0.72	0.76	78	SO4
2	461	0.63	0.76	32	empty
3	419	0.60	0.75	29	empty
4	100	0.49	0.81	20	empty
5	86	0.44	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 2373 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

6LF0 · Structure of FEM1C · the same entry in another collection · chain A against A, TM-score 1.00
Q96JP0 · AlphaFold monomer V2.0 prediction for protein fem-1 homolog C (Q96JP0) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 Q96JP0
Elsewhere: RCSB PDB 6LF0 · PDBe 6LF0 · UniProt Q96JP0

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