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Crystal structure of the S105A mutant of a carbon-carbon bond hydrolase, DXNB2 from sphingomonas wittichii RW1, in complex with 3- cl hopda

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

PDB: 4LXH
Type: protein
Length: 276 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
Ligands: C1E, NA
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mcp hydrolase (EC 3.7.1.8)	protein	276	42% helix, 18% strand	A5VAT9

Ligands and binding sites

C1E · (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid · ligand · chains A
NA · Sodium ion · metal · chains A

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

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	499	0.76	0.83	49	C1E

Compared structures

4LXH · Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from… · 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 4LXH · PDBe 4LXH · UniProt A5VAT9

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