MolNFT v1 · #22793 · protein

RH3 designed right-handed coiled coil trimer

1TGG: “RH3 designed right-handed coiled coil trimer”. X-ray diffraction, 3 ligands (ACE, NI, CL), 1 pocket (best druggability 0.29). MolNFT v1 #22793 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1TGG
Type: protein
Length: 99 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Right-handed coiled coil trimer
Ligands: ACE, NI, CL
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 94% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Right-handed coiled coil trimer	protein	33	94% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 3 copies · chains A, B, C
NI · Nickel (II) ion · metal · 3 copies · chains B
CL · Chloride ion · ion · 5 copies · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.29	0.74	10	empty

Interfaces

3 interfaces between chains.

A–B · 667 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 564 Å² buried · 1 hydrogen bond · protein-protein
A–C · 552 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 24 modified, 3 covalent (nonstandard, carboxylation, covalent ligand).

Compared structures

1TGG · RH3 designed right-handed coiled coil trimer · 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
Elsewhere: RCSB PDB 1TGG · PDBe 1TGG

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