MolNFT v1 · #103618 · protein

Human transthyretin (ttr) complexed with 16-alpha-bromo-estradiol

4PM1: “Human transthyretin (ttr) complexed with 16-alpha-bromo-estradiol”. X-ray diffraction, 1 ligand (ESZ), 3 pockets (best druggability 0.32). MolNFT v1 #103618 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4PM1
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: ESZ
Pockets: 3 · best druggability 0.32

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	117	6% helix, 50% strand	P02766
B	Transthyretin	protein	115	7% helix, 53% strand	P02766

Ligands and binding sites

ESZ · (14beta,16alpha,17alpha)-16-bromoestra-1,3,5(10)-triene-3,17-diol · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 2 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	68	0.32	0.75	15	empty
2	57	0.31	0.75	14	empty
3	56	0.29	0.75	14	EDO

Interfaces

1 interface between chains.

A–B · 924 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

4PM1 · Human transthyretin (TTR) complexed with 16-alpha-bromo-estradiol · 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 4PM1 · PDBe 4PM1 · UniProt P02766

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