MolNFT v1 · #26040 · protein

Crystal structure of TT1426 from thermus thermophilus HB8

1WD5 · Hypothetical protein TT1426: “Crystal structure of TT1426 from thermus thermophilus HB8”. X-ray diffraction, 1 pocket (best druggability 0.47). MolNFT v1 #26040 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1WD5
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TT1426
UniProt: Q5SIB2
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein TT1426	protein	208	43% helix, 24% strand	Q5SIB2

Ligands and binding sites

MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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	186	0.47	0.76	30	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

1WD5 · Crystal structure of TT1426 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 Q5SIB2
Elsewhere: RCSB PDB 1WD5 · PDBe 1WD5 · UniProt Q5SIB2

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