MolNFT v1 · #127747 · protein

Human ttr altered conformation from soaking in iron chloride.

5N5Q · Transthyretin: “Human ttr altered conformation from soaking in iron chloride.”. X-ray diffraction, 2 ligands (FFE, FE), 2 pockets (best druggability 0.70). MolNFT v1 #127747 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5N5Q
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: FFE, FE
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transthyretin	protein	116	5% helix, 49% strand	P02766

Ligands and binding sites

FFE · [bis(oxidanyl)-[tetrakis(oxidanyl)ferriooxy]ferrio]oxy-pentakis(oxidanyl)iron · ligand · chains A
FE · Fe (III) ion · metal · 5 copies · chains A, B
ACT · Acetate ion · additive · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	334	0.70	0.83	37	FE
2	86	0.37	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 703 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5N5Q · Human TTR altered conformation from soaking in iron chloride. · 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 5N5Q · PDBe 5N5Q · UniProt P02766

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