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Crystal structure of BUGH16BWT

Analyse Crystal structure of BUGH16BWT in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T9X
Type: protein
Length: 889 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase
Ligands: NA
Pockets: 5 · best druggability 0.84

Structure

x-ray diffraction · 3 distinct chains · 10% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase	protein	299	9% helix, 42% strand	—
B	Glycoside hydrolase	protein	296	12% helix, 43% strand	—
C	Glycoside hydrolase	protein	294	9% helix, 43% strand	—

Ligands and binding sites

NA · Sodium ion · metal · 3 copies · chains A, B, C
IMD · Imidazole · additive · 3 copies · chains A, B, C

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1140	0.84	0.85	111	IMD
2	419	0.73	0.83	41	IMD
3	532	0.67	0.77	42	IMD
4	123	0.40	0.75	20	empty
5	98	0.34	0.73	15	empty

Interfaces

3 interfaces between chains.

A–B · 801 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 737 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 69 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5T9X · Crystal structure of BuGH16Bwt · 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 5T9X · PDBe 5T9X

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