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Fusarium solani cutinase mutant with ser 129 replaced by cys complex with mercury acetate

Analyse Fusarium solani cutinase mutant with ser 129 replaced by cys complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XZB
Type: protein
Length: 197 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cutinase
EC: 3.1.1.-
UniProt: P00590
Ligands: MAC
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cutinase (EC 3.1.1.-)	protein	197	46% helix, 15% strand	P00590

Ligands and binding sites

MAC · Mercury acetate ion · ligand · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.32	0.77	18	empty

Modifications

Observed in the structure: 2 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

1XZB · Fusarium solani cutinase mutant with ser 129 replaced by cys complex with mercury acetate · the same entry in another collection · chain A against A, TM-score 1.00
P00590 · AlphaFold monomer V2.0 prediction for cutinase 1 (P00590) · a predicted model of the same protein · 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 P00590
Elsewhere: RCSB PDB 1XZB · PDBe 1XZB · UniProt P00590

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