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Structure of C. elegans htp-2 bound to him-3 closure motif, P212121 form

Analyse Structure of C. elegans htp-2 bound to him-3 closure motif, P212121 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TZS
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 him-3 closure motif
UniProt: Q95XC8, G5EBG0
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 3 distinct chains · 31% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein htp-2	protein	229	31% helix, 28% strand	Q95XC8
B	Protein htp-2	protein	230	33% helix, 27% strand	Q95XC8
C, D	C. elegans him-3 closure motif	protein	17	0% helix, 35% strand	G5EBG0

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	72	0.35	0.76	15	empty
2	72	0.35	0.76	21	empty

Interfaces

2 interfaces between chains.

B–D · 1185 Å² buried · 25 hydrogen bonds · protein-protein
A–C · 1183 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

4TZS · Structure of C. elegans HTP-2 bound to HIM-3 closure motif, P212121 form · 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 G5EBG0
Elsewhere: RCSB PDB 4TZS · PDBe 4TZS · UniProt Q95XC8 · UniProt G5EBG0

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