MolNFT v1 · #134633 · protein

Crystal structure of BUGH117BWT

5TA7 · Glycoside hydrolase: “Crystal structure of BUGH117BWT”. X-ray diffraction, 1 ligand (MG), 6 pockets (best druggability 0.76). MolNFT v1 #134633 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5TA7
Type: protein
Length: 739 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase
Ligands: MG
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase	protein	369	6% helix, 40% strand	—
B	Glycoside hydrolase	protein	370	6% helix, 40% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 11 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

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	879	0.76	0.80	101	TRS
2	340	0.67	0.81	29	EDO
3	181	0.60	0.83	23	empty
4	164	0.57	0.81	24	empty
5	82	0.37	0.77	16	empty

Interfaces

1 interface between chains.

A–B · 3398 Å² buried · 63 hydrogen bonds · protein-protein

Compared structures

5TA7 · Crystal structure of BuGH117Bwt · 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 5TA7 · PDBe 5TA7

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