MolNFT v1 · #125396 · protein

Crystal structure of BVGH123

5L7R · Glycoside hydrolase: “Crystal structure of BVGH123”. X-ray diffraction, 13 pockets (best druggability 0.78). MolNFT v1 #125396 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5L7R
Type: protein
Length: 1,126 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase
UniProt: A6L2E5
Pockets: 13 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glycoside hydrolase	protein	563	30% helix, 29% strand	A6L2E5

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	915	0.78	0.81	98	EDO
2	339	0.63	0.79	42	EDO
3	173	0.53	0.79	29	empty
4	192	0.53	0.78	23	empty
5	169	0.52	0.79	22	empty

Interfaces

1 interface between chains.

A–B · 287 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

5L7R · Crystal structure of BvGH123 · 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 A6L2E5
Elsewhere: RCSB PDB 5L7R · PDBe 5L7R · UniProt A6L2E5

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