MolNFT v1 · #134607 · protein

Crystal structure of BUGH2AWT

5T98 · Glycoside hydrolase: “Crystal structure of BUGH2AWT”. X-ray diffraction, 17 pockets (best druggability 0.77). MolNFT v1 #134607 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5T98
Type: protein
Length: 1,511 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase
Pockets: 17 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase	protein	756	15% helix, 40% strand	—
B	Glycoside hydrolase	protein	755	14% helix, 41% strand	—

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 16 copies · chains A, B
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B

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

Pockets

17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.77	0.98	25	empty
2	109	0.76	0.96	27	empty
3	469	0.72	0.82	49	empty
4	396	0.72	0.83	36	empty
5	50	0.71	0.99	21	EDO

Interfaces

1 interface between chains.

A–B · 45 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5T98 · Crystal structure of BuGH2Awt · 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
Elsewhere: RCSB PDB 5T98 · PDBe 5T98

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