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Structure of htp-2 bound to htp-3 motif-6

Analyse Structure of htp-2 bound to htp-3 motif-6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TZN
Type: protein
Length: 477 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein htp-2; Protein htp-3
UniProt: Q95XC8, O01820
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein htp-2	protein	227	33% helix, 27% strand	Q95XC8
B	Protein htp-2	protein	232	31% helix, 27% strand	Q95XC8
C, D	Protein htp-3	protein	9	0% helix, 33% strand	O01820

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	582	0.64	0.75	60	empty
2	94	0.44	0.79	13	empty
3	50	0.25	0.72	13	empty

Interfaces

3 interfaces between chains.

A–C · 846 Å² buried · 20 hydrogen bonds · protein-protein
B–D · 813 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 268 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4TZN · Structure of HTP-2 bound to HTP-3 motif-6 · 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 Q95XC8
Every structure of UniProt O01820
Elsewhere: RCSB PDB 4TZN · PDBe 4TZN · UniProt Q95XC8 · UniProt O01820

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