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TTHA1264/TTHA1265 complex

Analyse TTHA1264/TTHA1265 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V4Y
Type: protein
Length: 803 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Zinc-dependent peptidase; Putative zinc protease
UniProt: Q5SIU9, Q5SIV0
Ligands: ZN
Pockets: 9 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Zinc-dependent peptidase	protein	401	48% helix, 21% strand	Q5SIU9
A	Putative zinc protease	protein	402	49% helix, 19% strand	Q5SIV0

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1109	0.75	0.77	116	ZN
2	381	0.70	0.82	42	empty
3	725	0.68	0.76	77	empty
4	338	0.60	0.77	39	empty
5	109	0.58	0.86	20	empty

Interfaces

1 interface between chains.

B–A · 2266 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

7V4Y · TTHA1264/TTHA1265 complex · the same entry in another collection · chain B against B, 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
Every structure of UniProt Q5SIV0
Elsewhere: RCSB PDB 7V4Y · PDBe 7V4Y · UniProt Q5SIU9 · UniProt Q5SIV0

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