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Structure of NS11 bound FEM1C

Analyse Structure of NS11 bound FEM1C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LEN
Type: protein
Length: 765 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein fem-1 homolog C,NS11 peptide
UniProt: Q96JP0
Pockets: 8 · best druggability 0.55

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,NS11 peptide	protein	384	56% helix, 3% strand	Q96JP0
B	Protein fem-1 homolog C,NS11 peptide	protein	381	56% helix, 3% strand	Q96JP0

Pockets

8 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	216	0.55	0.78	27	empty
2	240	0.53	0.77	25	empty
3	91	0.48	0.81	22	empty
4	82	0.43	0.79	19	empty
5	199	0.41	0.72	17	empty

Interfaces

1 interface between chains.

A–B · 916 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6LEN · Structure of NS11 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 6LEN · PDBe 6LEN · UniProt Q96JP0

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