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The crystal structure of tat-P(T) (TP0957)

Analyse The crystal structure of tat-P(T) (TP0957) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3U65
Type: protein
Length: 631 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TP33 protein
UniProt: O83923
Ligands: SCN
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	TP33 protein	protein	317	52% helix, 20% strand	O83923
A	TP33 protein	protein	314	51% helix, 20% strand	O83923

Ligands and binding sites

SCN · Thiocyanate ion · ion · 3 copies · chains B, A
EDO · 1,2-ethanediol · additive · 3 copies · chains B, A

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	316	0.67	0.81	53	empty
2	260	0.65	0.82	46	empty
3	434	0.59	0.75	38	empty
4	71	0.33	0.75	12	empty

Interfaces

1 interface between chains.

B–A · 234 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3U65 · The Crystal Structure of Tat-P(T) (Tp0957) · 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 O83923
Elsewhere: RCSB PDB 3U65 · PDBe 3U65 · UniProt O83923

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