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V30M mutant human transthyretin (ttr) complexed with gc-1 (V30M:GC-1)

Analyse V30M mutant human transthyretin (ttr) complexed with gc-1 (V30M:GC-1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NES
Type: protein
Length: 231 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: B72
Pockets: 3 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	116	6% helix, 53% strand	P02766
B	Transthyretin	protein	115	6% helix, 51% strand	P02766

Ligands and binding sites

B72 · {4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}acetic acid · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.37	0.76	16	empty
2	60	0.30	0.75	15	empty
3	60	0.27	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 907 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

3NES · V30M mutant human transthyretin (TTR) complexed with GC-1 (V30M:GC-1) · the same entry in another collection · chain A against A, TM-score 1.00

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 P02766
Elsewhere: RCSB PDB 3NES · PDBe 3NES · UniProt P02766

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