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Crystal structure of TTHA0409, putatative DNA modification methylase from thermus thermophilus HB8- selenomethionine derivative

Analyse Crystal structure of TTHA0409, putatative DNA modification methylase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZIE
Type: protein
Length: 465 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative modification methylase
UniProt: Q5SL84
Pockets: 7 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative modification methylase	protein	233	37% helix, 26% strand	Q5SL84
B	Putative modification methylase	protein	232	36% helix, 23% strand	Q5SL84

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	266	0.57	0.77	36	empty
2	260	0.53	0.76	41	empty
3	160	0.52	0.79	26	empty
4	144	0.52	0.80	23	empty
5	77	0.48	0.83	19	empty

Interfaces

1 interface between chains.

A–B · 2495 Å² buried · 40 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2ZIE · Crystal Structure of TTHA0409, Putatative DNA Modification Methylase from Thermus… · 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 Q5SL84
Elsewhere: RCSB PDB 2ZIE · PDBe 2ZIE · UniProt Q5SL84

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