1O2F: PTS system, glucose-specific IIA component

Name: PDB 1O2F: Complex of enzyme iiaglc and iibglc phosphocarrier protein hpr from escherichia coli NMR, restrained regularized mean structure
Published: 2003-05-13
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Complex of enzyme iiaglc and iibglc phosphocarrier protein hpr from escherichia coli NMR, restrained regularized mean structure. Determined by solution NMR. Released 13 May 2003.

Method: Solution NMR
Organism: Escherichia coli
Chains: 2
Atoms: 1,697
Mol. weight: 27.48 kDa
Ligands: PO3
Released: 13 May 2003

Explore 1O2F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1O2F contains 11 α-helices and 20 β-strands across 2 chains. 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: 6 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	20-23	4	1
α-helix	24	1
β-strand	28-31	4	2
α-helix	33-35	3
α-helix	39-42	4
β-strand	48-54	7	2
β-strand	58-60	3	3
β-strand	65-70	6	2
β-strand	76-81	6	2
β-strand	86-90	5	2
β-strand	93	1	4
α-helix	95-98	4
β-strand	103-105	3	3
β-strand	112-113	2	2
β-strand	118-122	5	3
α-helix	124-130	7
β-strand	133	1	4
β-strand	136-140	5	2
α-helix	143-145	3
β-strand	149-151	3	1
β-strand	155-156	2	2
β-strand	162-166	5	1

Chain B: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	315-323	9
α-helix	326-328	3
β-strand	329-334	6	5
β-strand	339-343	5	5
α-helix	346-348	3
α-helix	351-356	6
β-strand	361-365	5	5
β-strand	368-372	5	5
α-helix	377-389	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PTS system, glucose-specific IIA component	A	protein	168	Escherichia coli	P69783 (AlphaFold model)
PTS system, glucose-specific IIBC component	B	protein	90	Escherichia coli	P69786 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1O2F_1 PTS system, glucose-specific IIA component (chains A)
GLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMV
APVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVI
EFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK

Sequence of entity 2 (B), FASTA

>1O2F_2 PTS system, glucose-specific IIBC component (chains B)
EDATEDAKATGTSEMAAALVAAFGGKENITNLDACITRLRVSVADVSKVDQAGLKKLGAA
GVVVAGSGVQAIFGTKSDNLKTEMDEYIRN

Ligands and cofactors

ID	Name	Formula	Copies
PO3	Phosphite ion	O3 P	1

Primary citation

Solution Structure of the Phosphoryl Transfer Complex between the Signal-transducing Protein IIAGlucose and the Cytoplasmic Domain of the Glucose Transporter IICBGlucose of the Escherichia coli Glucose Phosphotransferase System. Cai, M., Williams Jr., D.C., Wang, G. et al. J Biol Chem (2003) 278:25191-25206. DOI 10.1074/jbc.M302677200 · PubMed

Other PDB entries of the same protein (UniProt P69783 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1F3Z 1.98 Å, Iiaglc-ZN complex
1F3G 2.1 Å, Three-dimensional structure of the escherichia coli phosphocarrier protein III glc
2F3G 2.13 Å, Iiaglc crystal form III
1GLA 2.6 Å, Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase
1GLB 2.6 Å, Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase
1GLC 2.65 Å, Cation promoted association (CPA) of a regulatory and target protein is controlled by…
1GLD 2.93 Å, Cation promoted association (CPA) of a regulatory and target protein is controlled by…
1GLE 2.94 Å, Cation promoted association (CPA) of a regulatory and target protein is controlled by…
4JBW 3.91 Å, Crystal structure of E. coli maltose transporter MalFGK2 in complex with its regulatory…
1GGR Complex of enzyme iiaglc and the histidine-containing phosphocarrier protein hpr from…
2MP0 Protein Phosphorylation upon a Fleeting Encounter

Browse structure collections

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