MolNFT v1 · #59402 · protein

Crystal structure of an ALPHA/BETA hydrolase (YP_496220.1) from novosphingobium aromaticivorans dsm 12444 at 1.50 a resolution

3BWX: “Crystal structure of an ALPHA/BETA hydrolase (YP_496220.1) from novosphingobium aromaticivorans dsm 12444 at…”. X-ray diffraction, 2 ligands (CA, CL), 2 pockets (best druggability 0.78). MolNFT v1 #59402 on GenesisL1: 3D structure…

PDB: 3BWX
Type: protein
Length: 285 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA/BETA hydrolase
UniProt: Q2G9T7
Ligands: CA, CL
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA/BETA hydrolase	protein	285	38% helix, 21% strand	Q2G9T7

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 14 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	479	0.78	0.86	70	CA, CL, EDO
2	76	0.40	0.78	17	EDO

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3BWX · Crystal structure of an alpha/beta hydrolase (YP_496220.1) from Novosphingobium… · 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 Q2G9T7
Elsewhere: RCSB PDB 3BWX · PDBe 3BWX · UniProt Q2G9T7

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