1mt5 Summary

pdbe.org/1mt5
spacer

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

The structure was published by Bracey, M.H., Hanson, M.A., Masuda, K.R., Stevens, R.C., and Cravatt, B.F., in 2002 in a paper entitled "Structural Adaptations in a Membrane Enzyme That Terminates Endocannabinoid Signaling" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2002.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of Fatty-acid amide hydrolase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
B Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
C Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
D Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
E Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
F Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
G Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
H Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
I Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
J Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
K Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
L Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
M Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
N Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
O Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%
P Fatty-acid amide hydrolase P97612 (37-573) (FAAH1_RAT)search Rattus norvegicussearch 93% 537 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P97612 (37 - 573) Fatty-acid amide hydrolase Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P (P97612) Amidase signature (AS) enzymessearch Amidase signature (AS) enzymessearch PF01425: Amidasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P (P97612) fatty acid catabolic processsearch fatty acid metabolic processsearch fatty acid amide hydrolase activitysearch protein homodimerization activitysearch amidase activitysearch lipid bindingsearch carbon-nitrogen ligase activity, with glutamine as amido-N-donorsearch hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidessearch phospholipid bindingsearch hydrolase activity, acting on ester bondssearch hydrolase activitysearch organelle membranesearch integral component of membranesearch Golgi membranesearch endoplasmic reticulumsearch endoplasmic reticulum membranesearch Golgi apparatussearch membranesearch

Chain InterPro annotation
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P Amidasesearch Amidase, fungi typesearch Amidase, conserved sitesearch Amidase signature domainsearch