Research workbench

Crystal structure of the S105A mutant of a C-C hydrolase, DXNB2 from sphingomonas wittichii RW1

Analyse Crystal structure of the S105A mutant of a C-C hydrolase, DXNB2 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LYD
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mcp hydrolase
EC: 3.7.1.8
UniProt: A5VAT9
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mcp hydrolase (EC 3.7.1.8)	protein	268	43% helix, 19% strand	A5VAT9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	292	0.65	0.81	35	empty

Compared structures

4LYD · Crystal structure of the S105A mutant of a C-C hydrolase, DxnB2 from Sphingomonas… · 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 A5VAT9
Elsewhere: RCSB PDB 4LYD · PDBe 4LYD · UniProt A5VAT9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.