MolNFT v1 · #107092 · protein

C. elegans htp-2 bound to htp-3 closure motif 1

4TZM · Protein htp-2: “C. elegans htp-2 bound to htp-3 closure motif 1”. X-ray diffraction, 3 pockets (best druggability 0.61). MolNFT v1 #107092 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4TZM
Type: protein
Length: 493 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein htp-2; C. elegans htp-3 closure MOTIF1
UniProt: Q95XC8
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 4 distinct chains · 30% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein htp-2	protein	239	31% helix, 27% strand	Q95XC8
B	Protein htp-2	protein	227	33% helix, 27% strand	Q95XC8
C	C. elegans htp-3 closure MOTIF1	protein	13	0% helix, 54% strand	—
D	C. elegans htp-3 closure MOTIF1	protein	14	0% helix, 50% strand	—

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	396	0.61	0.77	47	empty
2	100	0.45	0.79	16	empty
3	84	0.40	0.78	11	empty

Interfaces

3 interfaces between chains.

B–D · 1112 Å² buried · 26 hydrogen bonds · protein-protein
A–C · 1085 Å² buried · 27 hydrogen bonds · protein-protein
A–B · 340 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4TZM · C. elegans HTP-2 bound to HTP-3 closure motif 1 · 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
Elsewhere: RCSB PDB 4TZM · PDBe 4TZM · UniProt Q95XC8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.