MolNFT v1 · #125550 · protein

Xray structure of mouse FAM3C ilei dimer

5LC4 · Protein FAM3C: “Xray structure of mouse FAM3C ilei dimer”. X-ray diffraction, 4 pockets (best druggability 0.67). MolNFT v1 #125550 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5LC4
Type: protein
Length: 679 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein FAM3C
UniProt: Q91VU0
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 13% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein FAM3C	protein	171	13% helix, 35% strand	Q91VU0
B	Protein FAM3C	protein	170	13% helix, 35% strand	Q91VU0
C, D	Protein FAM3C	protein	169	13% helix, 35% strand	Q91VU0

Pockets

4 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	330	0.67	0.81	55	empty
2	320	0.65	0.81	48	empty
3	168	0.52	0.79	23	empty
4	125	0.40	0.75	22	empty

Interfaces

2 interfaces between chains.

A–D · 3289 Å² buried · 73 hydrogen bonds · protein-protein
B–C · 3268 Å² buried · 75 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5LC4 · Xray structure of mouse FAM3C ILEI dimer · the same entry in another collection · chain D against D, TM-score 1.00
Q91VU0 · AlphaFold monomer V2.0 prediction for protein FAM3C (Q91VU0) · a predicted model of the same protein · chain C against A, TM-score 0.80

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 Q91VU0
Elsewhere: RCSB PDB 5LC4 · PDBe 5LC4 · UniProt Q91VU0

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