1GGR: Pts system, glucose-specific iia component

Name: PDB 1GGR: Complex of enzyme iiaglc and the histidine-containing phosphocarrier protein hpr from escherichia coli NMR, restrained regularized mean structure
Published: 2000-11-15
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Complex of enzyme iiaglc and the histidine-containing phosphocarrier protein hpr from escherichia coli NMR, restrained regularized mean structure. Determined by solution NMR. Released 15 Nov 2000.

Method: Solution NMR
Organism: Escherichia coli
Chains: 2
Atoms: 1,778
Mol. weight: 27.35 kDa
Ligands: PO3
Released: 15 Nov 2000

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

Secondary structure: helices and β-sheets

1GGR contains 9 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: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	302-307	6	5
α-helix	316-326	11
β-strand	332-337	6	5
β-strand	340-343	4	5
α-helix	347-350	4
β-strand	360-366	7	5
α-helix	370-383	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Pts system, glucose-specific iia component	A	protein	168	Escherichia coli	P69783 (AlphaFold model)
Phosphocarrier protein hpr	B	protein	85	Escherichia coli	P0AA04 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GGR_1 PTS SYSTEM, GLUCOSE-SPECIFIC IIA COMPONENT (chains A)
GLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMV
APVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVI
EFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK

Sequence of entity 2 (B), FASTA

>1GGR_2 PHOSPHOCARRIER PROTEIN HPR (chains B)
MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTV
VTISAEGEDEQKAVEHLVKLMAELE

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 proteins HPr and IIA(glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. Wang, G., Louis, J.M., Sondej, M. et al. EMBO J (2000) 19:5635-5649. DOI 10.1093/emboj/19.21.5635 · 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…
1O2F Complex of enzyme iiaglc and iibglc phosphocarrier protein hpr from escherichia coli…
2MP0 Protein Phosphorylation upon a Fleeting Encounter

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