6DII | pdb_00006dii

Structure of Arabidopsis Fatty Acid Amide Hydrolase in Complex with methyl linolenyl fluorophosphonate

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Amidase	e6diiA1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
B	Amidase	e6diiB1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
C	Amidase	e6diiC1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
D	Amidase	e6diiD1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
E	Amidase	e6diiE1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
F	Amidase	e6diiF1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
G	Amidase	e6diiG1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
H	Amidase	e6diiH1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
I	Amidase	e6diiI1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
J	Amidase	e6diiJ1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
K	Amidase	e6diiK1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
L	Amidase	e6diiL1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
L	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	PF01425	Amidase (Amidase)	Amidase	This entry represents the amidase signature domain that consists structurally of a core domain that is covered by alpha-helices. In most members, this is found as a standalone domain, while in others, such as Scytalone dehydratase-like protein Arp1, ...	This entry represents the amidase signature domain that consists structurally of a core domain that is covered by alpha-helices. In most members, this is found as a standalone domain, while in others, such as Scytalone dehydratase-like protein Arp1, it is found in association with other domains.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	Fatty acid amide hydrolase	N-(long-chain-acyl)ethanolamine deacylase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds fatty acid amide hydrolase activity	lipid catabolic process catabolic process metabolic process cellular process primary metabolic process lipid metabolic process N-acylethanolamine metabolic process amine metabolic process ethanolamine-containing compound metabolic process alcohol metabolic process small molecule metabolic process biogenic amine metabolic process primary alcohol metabolic process biological process involved in interspecies interaction between organisms lipid catabolic process catabolic process metabolic process cellular process primary metabolic process lipid metabolic process N-acylethanolamine metabolic process amine metabolic process ethanolamine-containing compound metabolic process alcohol metabolic process small molecule metabolic process biogenic amine metabolic process primary alcohol metabolic process biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure Golgi apparatus organelle cytoplasm intracellular membrane-bounded organelle endomembrane system plastid cell periphery plasma membrane membrane plant-type vacuole membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure Golgi apparatus organelle cytoplasm intracellular membrane-bounded organelle endomembrane system plastid cell periphery plasma membrane membrane plant-type vacuole vacuole endoplasmic reticulum organelle subcompartment endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR036928	Amidase signature (AS) superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR000120	Amidase	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR023631	Amidase signature domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR020556	Amidase, conserved site	Conserved Site

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	OPM				Amidase signature (AS) enzymes

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.