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Crystal structure of the conserved hypothetical protein TT1465 from thermus thermophilus HB8

Analyse Crystal structure of the conserved hypothetical protein TT1465 from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WEK
Type: protein
Length: 1,240 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TT1465
UniProt: Q5SHT6
Ligands: PO4
Pockets: 14 · best druggability 0.75

Structure

x-ray diffraction · 6 distinct chains · 50% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein TT1465	protein	208	52% helix, 16% strand	Q5SHT6
B	Hypothetical protein TT1465	protein	207	49% helix, 16% strand	Q5SHT6
C	Hypothetical protein TT1465	protein	206	49% helix, 17% strand	Q5SHT6
D	Hypothetical protein TT1465	protein	208	49% helix, 16% strand	Q5SHT6
E	Hypothetical protein TT1465	protein	206	48% helix, 17% strand	Q5SHT6
F	Hypothetical protein TT1465	protein	205	50% helix, 16% strand	Q5SHT6

Ligands and binding sites

PO4 · Phosphate ion · ion · 12 copies · chains A, B, C, D, E, F

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

14 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	593	0.75	0.82	71	PO4
2	231	0.73	0.88	38	PO4
3	309	0.71	0.84	40	PO4
4	283	0.66	0.81	30	empty
5	239	0.63	0.82	34	PO4

Interfaces

13 interfaces between chains.

C–D · 2783 Å² buried · 26 hydrogen bonds · protein-protein
E–F · 2752 Å² buried · 22 hydrogen bonds · protein-protein
A–B · 2663 Å² buried · 24 hydrogen bonds · protein-protein
D–E · 651 Å² buried · 14 hydrogen bonds · protein-protein
A–F · 498 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

1WEK · Crystal structure of the conserved hypothetical protein TT1465 from Thermus thermophilus… · 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 Q5SHT6
Elsewhere: RCSB PDB 1WEK · PDBe 1WEK · UniProt Q5SHT6

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