MolNFT v1 · #103631 · protein

Human transthyretin (ttr) complexed with curcumin

4PMF: “Human transthyretin (ttr) complexed with curcumin”. X-ray diffraction, 2 ligands (CUR, NA), 3 pockets (best druggability 0.35). MolNFT v1 #103631 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4PMF
Type: protein
Length: 234 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: CUR, NA
Pockets: 3 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transthyretin	protein	117	6% helix, 50% strand	P02766

Ligands and binding sites

CUR · (1Z,4Z,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · chains A
EDO · 1,2-ethanediol · additive · chains 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	75	0.35	0.76	17	empty
2	80	0.32	0.73	19	empty
3	65	0.29	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 933 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

4PMF · Human transthyretin (TTR) complexed with curcumin · 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 4PMF · PDBe 4PMF · UniProt P02766

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