MolNFT v1 · #35277 · protein

X-ray structure of thermus thermopilus HB8 TT0505

2E6K · Transketolase: “X-ray structure of thermus thermopilus HB8 TT0505”. X-ray diffraction, 20 pockets (best druggability 0.77). MolNFT v1 #35277 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2E6K
Type: protein
Length: 2,588 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transketolase
EC: 2.2.1.1
UniProt: Q5SM35
Pockets: 20 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transketolase (EC 2.2.1.1)	protein	647	45% helix, 14% strand	Q5SM35

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	356	0.77	0.87	57	empty
2	330	0.76	0.87	55	empty
3	327	0.75	0.87	48	empty
4	315	0.72	0.85	48	empty
5	323	0.67	0.82	49	empty

Interfaces

4 interfaces between chains.

C–D · 4004 Å² buried · 73 hydrogen bonds · protein-protein
A–B · 3980 Å² buried · 77 hydrogen bonds · protein-protein
B–C · 130 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 22 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 60 modified (engineered).

Compared structures

2E6K · X-ray structure of Thermus thermopilus HB8 TT0505 · 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 Q5SM35
Elsewhere: RCSB PDB 2E6K · PDBe 2E6K · UniProt Q5SM35

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