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Cgt structure in hexamer

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

PDB: 5HEA
Type: protein
Length: 828 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glycosyltransferase (GALT1)
UniProt: I1ZPA1
Pockets: 9 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Putative glycosyltransferase (GALT1)	protein	276	43% helix, 22% strand	I1ZPA1

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	737	0.68	0.75	50	empty
2	305	0.61	0.79	37	empty
3	254	0.52	0.76	26	empty
4	258	0.52	0.75	33	empty
5	222	0.51	0.76	24	empty

Interfaces

3 interfaces between chains.

B–C · 1723 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 364 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 73 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

5HEA · CgT structure in hexamer · 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 I1ZPA1
Elsewhere: RCSB PDB 5HEA · PDBe 5HEA · UniProt I1ZPA1

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