2HWG: Phosphoenolpyruvate-protein phosphotransferase

Name: PDB 2HWG: Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system
Published: 2006-11-14
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system. Determined by X-ray diffraction at 2.7 Å resolution. Released 14 Nov 2006.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Escherichia coli
Chains: 2
Atoms: 9,102
Mol. weight: 129.34 kDa
Ligands: MG, OXL
Released: 14 Nov 2006

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

Secondary structure: helices and β-sheets

2HWG contains 66 α-helices and 34 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: 33 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	1
β-strand	11-18	8	1
α-helix	30-32	3
α-helix	35-59	25
α-helix	61-64	4
α-helix	67-81	15
α-helix	83-94	12
α-helix	100-117	18
α-helix	121-141	21
α-helix	149-151	3
β-strand	156-160	5	1
α-helix	165-169	5
β-strand	176-181	6	1
α-helix	189-196	8
β-strand	201-203	3	1
α-helix	208-211	4
β-strand	217-221	5	1
β-strand	226-229	4	1
α-helix	233-253	21
α-helix	254-256	3
β-strand	262	1	2
β-strand	268	1	2
β-strand	270-275	6	3
α-helix	279-286	8
β-strand	292-296	5	3
α-helix	297-301	5
α-helix	310-323	14
β-strand	329-332	4	3
α-helix	333-334	2
α-helix	343-345	3
α-helix	347-349	3
α-helix	353-355	3
α-helix	360-363	4
α-helix	367-380	14
β-strand	386-390	5	3
α-helix	396-415	20
β-strand	425-430	6	3
α-helix	433-437	5
α-helix	439-443	5
β-strand	448-451	4	3
α-helix	453-461	9
α-helix	468-473	6
α-helix	479-494	16
β-strand	498-501	4	3
α-helix	512-517	6
β-strand	522-525	4	3
α-helix	527-529	3
α-helix	530-538	9
α-helix	542-554	13
α-helix	558-572	15

Chain B: 33 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	6-8	3	4
β-strand	10-18	9	4
α-helix	21-23	3
α-helix	35-58	24
α-helix	60-62	3
α-helix	69-80	12
α-helix	83-96	14
α-helix	100-116	17
α-helix	121-142	22
β-strand	156-160	5	4
α-helix	165-170	6
β-strand	176-181	6	4
α-helix	189-196	8
β-strand	201-202	2	4
α-helix	208-210	3
β-strand	217-222	6	4
β-strand	226-229	4	4
α-helix	233-253	21
α-helix	254-256	3
β-strand	262	1	5
β-strand	268	1	5
β-strand	270-275	6	6
α-helix	280-287	8
β-strand	292-296	5	6
α-helix	298-303	6
α-helix	310-323	14
β-strand	329-332	4	6
α-helix	333-334	2
α-helix	343-345	3
α-helix	353-355	3
α-helix	360-365	6
α-helix	367-380	14
β-strand	386-390	5	6
α-helix	396-415	20
β-strand	425-430	6	6
α-helix	433-437	5
α-helix	439-442	4
β-strand	448-451	4	6
α-helix	453-460	8
α-helix	468-473	6
α-helix	479-494	16
β-strand	498-501	4	6
α-helix	504-507	4
α-helix	509-511	3
α-helix	512-517	6
β-strand	522-525	4	6
α-helix	527-529	3
α-helix	530-538	9
α-helix	542-552	11
α-helix	558-572	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phosphoenolpyruvate-protein phosphotransferase	A, B	protein	575	Escherichia coli	P08839 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2HWG_1 Phosphoenolpyruvate-protein phosphotransferase (chains A, B)
MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTK
AGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD
EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFI
TDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR
AVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFL
FMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI
RIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAF
DESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS
VLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNT
NFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
OXL	Oxalate ion	C2 O4	2

Primary citation

Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein. Teplyakov, A., Lim, K., Zhu, P.P. et al. Proc Natl Acad Sci U S A (2006) 103:16218-16223. DOI 10.1073/pnas.0607587103 · PubMed

Other PDB entries of the same protein (UniProt P08839 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6V9K 1.9 Å, Crystal structure of the hybrid C-terminal domain of enzyme I of the bacterial…
1ZYM 2.5 Å, Amino terminal domain of enzyme I from escherichia coli
6VU0 3.5 Å, Crystal structure of the C-terminal domain of enzyme I of the bacterial…
1EZA Amino terminal domain of enzyme I from escherichia coli NMR, restrained regularized mean…
1EZB Amino terminal domain of enzyme I from escherichia coli, NMR, 17 structures
1EZC Amino terminal domain of enzyme I from escherichia coli, NMR, 17 structures
1EZD Amino terminal domain of enzyme I from escherichia coli NMR, 16 structures
2EZA Amino terminal domain of enzyme I from escherichia coli, NMR, restrained regularized…
2EZB Amino terminal domain of enzyme I from escherichia coli, NMR, 14 structures
2EZC Amino terminal domain of enzyme I from escherichia coli, NMR, 14 structures
2KX9 Solution Structure of the Enzyme I dimer Using Residual Dipolar Couplings and Small…
2L5H Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar…

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