Het-PDB Navi2 (PDB: 1XZM)

The number of atoms exceeds 100,000.
So, it can not be displayed here.

Select unit:

Select hetatm:

information

centroid:

interaction residue:

Select chain: Sequence Hide other chain(s)

Data format:

Color scheme of protein:

Ligands
Code	Name		Style	Show	Link
DPE	N-undecanylphosphonate methyl ester group				PoSSuM

Non-standard Residues
Code	Name	Show

Glycosylation
Code	Name	Emphasize

Modification
Code	Name	Show

Download interaction data: 1XZM

Code :

1XZM PDBj RCSB PDB PDBe

Header :

HYDROLASE (SERINE ESTERASE)

Title :

FUSARIUM SOLANI CUTINASE COMPLEX WITH N-UNDECYL O-METHYL CHLORO PHOSPHONATE ESTER

Release Data :

1996-11-30

Compound :

mol_id	molecule	chains
1	CUTINASE	A
	ec: 3.1.1.- other_details: COMPLEX WITH N-UNDECYL O-METHYL CHLORO PHOSPHONATE ESTER

Source :

mol_id	organism_scientific	expression_system
1	Nectria haematococca mpVI (taxid:70791)	Escherichia coli (taxid:562)
	strain: mpVI expression_system_plasmid: PUC 19

Authors :

Longhi, S., Nicolas, A., Cambillau, C.

Keywords :

HYDROLASE, SERINE ESTERASE, GLYCOPROTEIN, HYDROLASE (SERINE ESTERASE)

Exp. method :

X-RAY DIFFRACTION ( 1.75 Å )

Citation :

Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants.

Longhi, S.,Nicolas, A.,Creveld, L. et al.
(1996) Proteins 26 : 442 - 458

PubMed: 8990497
DOI: 10.1002/(SICI)1097-0134(199612)26:4<442::AID-PROT5>3.3.CO;2-H

Contribution of Cutinase Serine 42 Side Chain to the Stabilization of the Oxyanion Transition State

Nicolas, A.,Egmond, M.,Verrips, C.T. et al.
(1996) Biochemistry 35 : 398

Cutinase, a Lipolytic Enzyme with a Preformed Oxyanion Hole

Martinez, C.,Nicolas, A.,Van Tilbeurgh, H. et al.
(1994) Biochemistry 33 : 83

Engineering Cysteine Mutants to Obtain Crystallographic Phases with a Cutinase from Fusarium Solani Pisi

Martinez, C.,De Geus, P.,Stanssens, P. et al.
(1993) Protein Eng. 6 : 157

Fusarium Solani Cutinase is a Lipolytic Enzyme with a Catalytic Serine Accessible to Solvent

Martinez, C.,De Geus, P.,Lauwereys, M. et al.
(1992) Nature 356 : 615

Chain :

UniProt :

P00590 (CUTI1_FUSVN)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
cutin + H2O = cutin monomers.	3.1.1.74	PROSITE-ProRule:PRU10108, PROSITE- ProRule:PRU10109, PubMed:18658138, PubMed:19810726, PubMed:8286366, PubMed:8555209
cutin + H2O = cutin monomers.	-

PDB ID: 1XZM

Hetero Atom Contents

Structure summary

Reaction