MolNFT v1 · #54434 · protein

High resolution structure of ttrd from archaeoglobus fulgidus

2XOL · Chaperone protein ttrd: “High resolution structure of ttrd from archaeoglobus fulgidus”. X-ray diffraction, 2 pockets (best druggability 0.70). MolNFT v1 #54434 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2XOL
Type: protein
Length: 340 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein ttrd
UniProt: O30077
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein ttrd	protein	168	72% helix, 1% strand	O30077
B	Chaperone protein ttrd	protein	172	71% helix, 1% strand	O30077

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A

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	51	0.70	0.98	14	empty
2	106	0.38	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 1124 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2XOL · High resolution structure of TtrD from Archaeoglobus fulgidus · the same entry in another collection · chain A against A, TM-score 1.00
O30077 · AlphaFold monomer V2.0 prediction for tat proofreading chaperone ttrd (O30077) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O30077
Elsewhere: RCSB PDB 2XOL · PDBe 2XOL · UniProt O30077

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