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Structure of TTHA1265

Analyse Structure of TTHA1265 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HXK
Type: protein
Length: 1,208 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Molecule: Zinc-dependent peptidase
UniProt: Q5SIU9
Pockets: 19 · best druggability 0.72

Structure

x-ray diffraction · resolution 2 · 2 distinct chains · 48% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zinc-dependent peptidase	protein	404	49% helix, 20% strand	Q5SIU9
B, C	Zinc-dependent peptidase	protein	402	48% helix, 20% strand	Q5SIU9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	386	0.72	0.83	54	empty
2	815	0.70	0.76	67	empty
3	322	0.68	0.82	41	empty
4	527	0.66	0.77	58	empty
5	519	0.65	0.77	60	empty

Interfaces

2 interfaces between chains.

B–C · 2616 Å² buried · 34 hydrogen bonds · protein-protein
A–B · 573 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5HXK · Structure of TTHA1265 · 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 Q5SIU9
Elsewhere: RCSB PDB 5HXK · PDBe 5HXK · UniProt Q5SIU9

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