1MLA: PDB entry 1MLA

The escherichia coli malonyl-coa:acyl carrier protein transacylase at 1.5-Å resolution. Crystal structure of a fatty acid synthase component. Determined by X-ray diffraction at 1.5 Å resolution. Released 8 Mar 1996.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Escherichia coli
Chains
1
Atoms
2,408
Mol. weight
32.44 kDa
Released
8 Mar 1996

Explore 1MLA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MLA contains 17 α-helices and 12 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 17 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand4-851
α-helix20-256
α-helix27-4014
α-helix44-507
α-helix53-564
α-helix59-7921
α-helix82-854
β-strand87-9041
α-helix93-1019
α-helix107-12418
β-strand130-13672
α-helix140-15011
β-strand156-16382
β-strand166-17272
α-helix173-18513
β-strand190-19342
α-helix1941
α-helix203-2053
α-helix206-21712
β-strand22811
β-strand22913
β-strand23613
α-helix240-25213
β-strand255-25622
α-helix257-26610
β-strand271-27441
α-helix280-2889
β-strand293-29641
α-helix300-3067

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Malonyl-coenzyme a acyl carrier protein transacylaseAprotein309Escherichia coliP0AAI9 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1MLA_1 MALONYL-COENZYME A ACYL CARRIER PROTEIN TRANSACYLASE (chains A)
MTQFAFVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELNKTW
QTQPALLTASVALYRVWQQQGGKAPAMMAGHSLGEYSALVCAGVIDFADAVRLVEMRGKF
MQEAVPEGTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVERAG
AACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFNAPTVPVVNNVDVKCETNG
DAIRDALVRQLYNPVQWTKSVEYMAAQGVEHLYEVGPGKVLTGLTKRIVDTLTASALNEP
SAMAAALEL

Primary citation

The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component. Serre, L., Verbree, E.C., Dauter, Z. et al. J Biol Chem (1995) 270:12961-12964. DOI 10.1074/jbc.270.22.12961 · PubMed

Other PDB entries of the same protein (UniProt P0AAI9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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