Alpha/beta hydrolase fold

Alpha/beta hydrolase fold

Pfam_box
Symbol = Abhydrolase_1
Name =


width =250
caption = A bacterial lipase, one of this family members
Pfam= PF00561
InterPro= IPR000073
SMART=
Prosite =
SCOP = 1ede
TCDB =
OPM family= 135
OPM protein= 1qge
PDB=PDB3|1q0zA:52-292 PDB3|1q0rA:52-292 PDB3|1y7iA:32-106PDB3|1xklB:32-106 PDB3|1y7hA:32-106 PDB3|1eb8A:31-252PDB3|1dwqA:31-252 PDB3|1e89B:31-252 PDB3|1e8dA:31-252PDB3|1dwoA:31-252 PDB3|1dwpA:31-252 PDB3|1eb9B:31-252PDB3|1sc9A:31-251 PDB3|6yasA:31-251 PDB3|1sckA:31-251PDB3|3yasA:31-251 PDB3|1sciA:31-251 PDB3|5yasA:31-251PDB3|7yasA:31-251 PDB3|1qj4A:31-251 PDB3|1yb7A:31-251PDB3|4yasA:31-251 PDB3|1scqA:31-251 PDB3|2yasA:31-251PDB3|1yb6A:31-251 PDB3|1m33A:40-251 PDB3|1a88C:50-272PDB3|1a8s :48-270 PDB3|1a8q :48-271 PDB3|1va4E:48-268PDB3|1a7uA:52-274 PDB3|1a8uA:52-274 PDB3|1broB:52-274PDB3|1brt :52-274 PDB3|1hl7B:52-276 PDB3|1hkhA:52-276PDB3|1u2eD:71-288 PDB3|1ukbA:55-268 PDB3|1uk7A:55-268PDB3|1uk9A:55-268 PDB3|1c4xA:59-280 PDB3|1j1iA:66-277PDB3|1qtrA:64-315 PDB3|1wm1A:64-315 PDB3|1azwA:61-308PDB3|1r3dA:43-256 PDB3|1ehyD:56-291 PDB3|1qo7B:142-201PDB3|2eda :75-305 PDB3|1ede :75-305 PDB3|1bez :75-305PDB3|1bn6A:59-288 PDB3|1cqwA:59-288 PDB3|1bn7A:59-288PDB3|1mj5A:56-288 PDB3|1d07A:56-288 PDB3|1womB:45-263PDB3|1wprB:45-263 PDB3|1xqxA:56-287 PDB3|1xrmA:56-287PDB3|1xrqA:56-287 PDB3|1mt3A:56-287 PDB3|1xqwA:56-287PDB3|2b61A:92-353 PDB3|1tahD:81-334 PDB3|1qgeD:81-261PDB3|1cvl :81-334 PDB3|4lipE:86-340 PDB3|3lip :86-340PDB3|1ex9A:45-290 PDB3|1i6wB:78-117 PDB3|1r50A:78-117PDB3|1r4zB:78-117 PDB3|1t4mA:78-117 PDB3|1t2nA:78-117PDB3|1ispA:78-117 PDB3|1hlgB:111-391 PDB3|1k8qA:111-392PDB3|1s8oA:286-540 PDB3|1vj5A:286-540 PDB3|1cr6A:284-539

The alpha/beta hydrolase foldcite journal |author=Remington SJ, Franken SM, Frolow F, Ollis DL, Cheah E, Cygler M, Dijkstra B, Harel M, Silman I, Schrag J |title=The alpha/beta hydrolase fold |journal=Protein Eng. |volume=5 |issue=3 |pages=197–211 |year=1992 |pmid=1409539 |doi=10.1093/protein/5.3.197] is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 strands connected byhelices. The enzymes are believed to have diverged from a common ancestor, preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best conserved structural features of the fold.

This catalytic domain is found in a very wide range of enzymes.

Subfamilies

*3-oxoadipate enol-lactonase InterPro|IPR012790

Human proteins containing this domain

ABHD10; ABHD11; ABHD12; ABHD12B; ABHD13; ABHD2; ABHD3; ABHD4;
ABHD5; ABHD6; ABHD7; ABHD8; ABHD9; BAT5; BPHL; C20orf135;
EPHX1; EPHX2; FAM108B1; LIPA; LIPF; LIPJ; LIPK; LIPM;
LIPN; MEST; MGLL; PPME1; SERHL; SERHL2; SPG21;

References


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