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HYDRA FAM20

Analyse HYDRA FAM20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XOM
Type: protein
Length: 702 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosaminoglycan xylosylkinase
UniProt: T2MHS6
Ligands: NAG
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glycosaminoglycan xylosylkinase	protein	351	37% helix, 18% strand	T2MHS6

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B

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

Pockets

6 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	54	0.72	0.99	18	empty
2	51	0.71	0.99	18	empty
3	364	0.63	0.78	45	empty
4	385	0.61	0.77	48	empty
5	69	0.61	0.91	22	empty

Interfaces

1 interface between chains.

A–B · 860 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

5XOM · Hydra Fam20 · 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 T2MHS6
Elsewhere: RCSB PDB 5XOM · PDBe 5XOM · UniProt T2MHS6

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