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Fusarium solani cutinase complex with N-undecyl O-methyl chloro phosphonate ester

Analyse Fusarium solani cutinase complex with N-undecyl O-methyl chloro phosphonate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XZM
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: DPE
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cutinase (EC 3.1.1.-)	protein	197	44% helix, 15% strand	P00590

Ligands and binding sites

DPE · N-undecanylphosphonate methyl ester group · ligand · 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	56	0.33	0.77	19	DPE

Modifications

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

Compared structures

1XZM · Fusarium solani cutinase complex with N-undecyl O-methyl chloro phosphonate ester · 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 1XZM · PDBe 1XZM · UniProt P00590

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