MolNFT v1 · #155649 · protein

Structure of lnlptqgrar bound FEM1C

6LE6 · Protein fem-1 homolog C,10-mer peptide: “Structure of lnlptqgrar bound FEM1C”. X-ray diffraction, 1 ligand (SO4), 7 pockets (best druggability 0.70). MolNFT v1 #155649 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6LE6
Type: protein
Length: 770 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein fem-1 homolog C,10-mer peptide
UniProt: Q96JP0
Ligands: SO4
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein fem-1 homolog C,10-mer peptide	protein	392	55% helix, 3% strand	Q96JP0
B	Protein fem-1 homolog C,10-mer peptide	protein	378	56% helix, 3% strand	Q96JP0

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	972	0.70	0.75	68	SO4
2	363	0.62	0.78	43	empty
3	121	0.60	0.85	24	empty
4	147	0.56	0.81	26	empty
5	166	0.46	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 1074 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6LE6 · Structure of LNLPTQGRAR bound 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 0.97

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 6LE6 · PDBe 6LE6 · UniProt Q96JP0

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