2G2Z: E.coli FabD

Structure of E.coli FabD complexed with malonyl-CoA. Determined by X-ray diffraction at 2.8 Å resolution. Released 27 Jun 2006.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Escherichia coli
Chains: 1
Atoms: 2,322
Mol. weight: 33.18 kDa
Ligands: MLA, COZ
Released: 27 Jun 2006

Explore 2G2Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2G2Z contains 17 α-helices and 10 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, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	1
α-helix	20-25	6
α-helix	28-40	13
α-helix	44-50	7
α-helix	53-56	4
α-helix	59-79	21
α-helix	82-85	4
β-strand	87-90	4	1
α-helix	94-101	8
α-helix	107-124	18
β-strand	130-136	7	2
α-helix	140-150	11
β-strand	156-163	8	2
β-strand	166-172	7	2
α-helix	173-185	13
β-strand	190-194	5	2
α-helix	203-205	3
α-helix	206-216	11
α-helix	222-224	3
β-strand	228	1	1
α-helix	240-250	11
β-strand	255-256	2	2
α-helix	257-265	9
β-strand	271-274	4	1
α-helix	280-288	9
β-strand	293-296	4	1
α-helix	300-306	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Malonyl CoA-acyl carrier protein transacylase	A	protein	308	Escherichia coli	P0AAI9 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2G2Z_1 Malonyl CoA-acyl carrier protein transacylase (chains A)
TQFAFVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELNKTWQ
TQPALLTASVALYRVWQQQGGKAPAMMAGHSLGEYSALVCAGVIDFADAVRLVEMRGKFM
QEAVPEGTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVERAGA
ACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFNAPTVPVVNNVDVKCETNGD
AIRDALVRQLYNPVQWTKSVEYMAAQGVEHLYEVGPGKVLTGLTKRIVDTLTASALNEPS
AMAAALEL

Ligands and cofactors

ID	Name	Formula	Copies
MLA	Malonic acid	C3 H4 O4	1
COZ	Coenzyme a	C21 H36 N7 O16 P3 S	1

Primary citation

Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography. Oefner, C., Schulz, H., D'Arcy, A. et al. Acta Crystallogr D Biol Crystallogr (2006) 62:613-618. DOI 10.1107/S0907444906009474 · PubMed

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

1MLA 1.5 Å, The escherichia coli malonyl-coa:acyl carrier protein transacylase at 1.5-Å resolution.…
2G2O 1.76 Å, Structure of E.coli FabD complexed with sulfate
2G1H 1.86 Å, Structure of E.coli FabD complexed with glycerol
6U0J 1.9 Å, Crosslinked Crystal Structure of Malonyl-CoA Acyl Carrier Protein Transacylase, FabD,…
2G2Y 2.26 Å, Structure of E.coli FabD complexed with malonate

Browse structure collections

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