1GLC: Glucose-specific protein iiiglc

Cation promoted association (CPA) of a regulatory and target protein is controlled by phosphorylation. Determined by X-ray diffraction at 2.65 Å resolution. Released 31 May 1994.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Escherichia coli
Chains: 2
Atoms: 4,990
Mol. weight: 74.99 kDa
Ligands: ADP, G3H, MG, ZN
Released: 31 May 1994

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

Secondary structure: helices and β-sheets

1GLC contains 28 α-helices and 49 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 F: 5 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	20-23	4	1
β-strand	28-29	2	2
β-strand	30-32	3	3
α-helix	33-35	3
α-helix	39-42	4
β-strand	48-52	5	3
β-strand	58-60	3	4
β-strand	65-70	6	3
β-strand	76-81	6	3
β-strand	86-90	5	3
β-strand	93	1	5
α-helix	95-98	4
β-strand	101	1	4
β-strand	103-105	3	4
β-strand	112-113	2	3
β-strand	118-122	5	4
α-helix	126-130	5
β-strand	133	1	5
β-strand	138-140	3	3
α-helix	143-145	3
β-strand	148-151	4	1
β-strand	155-156	2	2
β-strand	162-167	6	1

Chain G: 23 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	6
β-strand	15	1	7
β-strand	16-22	7	6
β-strand	27-31	5	6
β-strand	34	1	7
β-strand	38	1	8
β-strand	46-47	2	8
α-helix	49-67	19
β-strand	74-81	8	6
β-strand	86-90	5	8
β-strand	95-96	2	8
α-helix	99	1
β-strand	100-101	2	8
α-helix	102	1
α-helix	109-118	10
α-helix	120-128	9
α-helix	137-146	10
α-helix	152-156	5
β-strand	160-164	5	8
α-helix	165-173	9
β-strand	180-182	3	9
α-helix	183-187	5
β-strand	192-193	2	10
β-strand	198-199	2	10
α-helix	201-206	6
β-strand	216-218	3	9
β-strand	221-226	6	6
β-strand	238-244	7	6
α-helix	245-252	8
β-strand	261-265	5	11
β-strand	269-274	6	11
α-helix	280-282	3
α-helix	286	1
β-strand	287-293	7	11
β-strand	297-306	10	11
α-helix	310-315	6
α-helix	316-320	5
α-helix	328-333	6
β-strand	343-345	3	12
β-strand	348	1	13
β-strand	350	1	13
β-strand	351	1	14
β-strand	357	1	14
β-strand	363-365	3	12
α-helix	373-399	27
β-strand	405-409	5	11
α-helix	412-414	3
α-helix	416-426	11
β-strand	429-433	5	11
α-helix	438-450	13
α-helix	457-460	4
β-strand	466-470	5	11
α-helix	474-477	4
α-helix	479-493	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glucose-specific protein iiiglc	F	protein	168	Escherichia coli	P69783 (AlphaFold model)
Glycerol kinase	G	protein	501	Escherichia coli	P0A6F3 (AlphaFold model)

Sequence of entity 1 (F), FASTA

>1GLC_1 GLUCOSE-SPECIFIC PROTEIN IIIGlc (chains F)
GLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMV
APVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVI
EFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK

Sequence of entity 2 (G), FASTA

>1GLC_2 GLYCEROL KINASE (chains G)
TEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTL
VEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGL
EDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHV
TDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPIS
GIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNY
ALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYA
RGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQ
FQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERN
YRYAGWKKAVKRAMAWEEHDE

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
G3H	Glyceraldehyde-3-phosphate	C3 H7 O6 P	1
MG	Magnesium ion	Mg	1
ZN	Zinc ion	Zn	1

Primary citation

Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Feese, M., Pettigrew, D.W., Meadow, N.D. et al. Proc Natl Acad Sci U S A (1994) 91:3544-3548. DOI 10.1073/pnas.91.9.3544 · 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
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…
1O2F Complex of enzyme iiaglc and iibglc phosphocarrier protein hpr from escherichia coli…
2MP0 Protein Phosphorylation upon a Fleeting Encounter

Browse structure collections

About this viewer

MolViewer shows 1GLC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.