MolNFT v1 · #35685 · protein

X-ray structure of acyl-CoA hydrolase-like protein, TT1379, from thermus thermophilus HB8

2EIS · Hypothetical protein TTHB207: “X-ray structure of acyl-CoA hydrolase-like protein, TT1379, from thermus thermophilus HB8”. X-ray diffraction, 1 ligand (COA), 1 pocket (best druggability 0.39). MolNFT v1 #35685 on GenesisL1: 3D…

PDB: 2EIS
Type: protein
Length: 242 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TTHB207
UniProt: Q53VX2
Ligands: COA
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein TTHB207	protein	121	19% helix, 46% strand	Q53VX2

Ligands and binding sites

COA · Coenzyme A · ligand · 2 copies · chains A, 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	114	0.39	0.75	24	empty

Interfaces

1 interface between chains.

A–B · 894 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2EIS · X-ray structure of acyl-CoA hydrolase-like protein, TT1379, from Thermus thermophilus HB8 · 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 Q53VX2
Elsewhere: RCSB PDB 2EIS · PDBe 2EIS · UniProt Q53VX2

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