1ZYM: Enzyme I

Name: PDB 1ZYM: Amino terminal domain of enzyme I from escherichia coli
Published: 1996-12-07
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: phosphotransferase

Amino terminal domain of enzyme I from escherichia coli. Determined by X-ray diffraction at 2.5 Å resolution. Released 7 Dec 1996.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Escherichia coli
Chains: 2
Atoms: 3,854
Mol. weight: 56.45 kDa
Released: 7 Dec 1996

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

Secondary structure: helices and β-sheets

1ZYM contains 26 α-helices and 17 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: 14 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	8	1	1
β-strand	12-18	7	1
α-helix	36-65	30
α-helix	67-80	14
α-helix	83-96	14
α-helix	100-112	13
α-helix	121-142	22
α-helix	144-146	3
α-helix	149-151	3
β-strand	156-159	4	1
α-helix	165-170	6
α-helix	173-175	3
β-strand	176-180	5	1
α-helix	189-197	9
β-strand	201-202	2	1
α-helix	208-211	4
β-strand	217-220	4	1
β-strand	227-229	3	1
α-helix	233-237	5
α-helix	238-243	6
α-helix	244-247	4

Chain B: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	8	1	2
β-strand	11-15	5	3
β-strand	16-18	3	2
β-strand	30	1	4
α-helix	36-63	28
α-helix	66-80	15
α-helix	83-94	12
β-strand	98	1	4
α-helix	100-115	16
α-helix	121-142	22
α-helix	145-147	3
α-helix	149-151	3
β-strand	156-159	4	2
α-helix	165-168	4
β-strand	176-180	5	2
α-helix	189-197	9
β-strand	201-202	2	2
α-helix	208-210	3
β-strand	217-221	5	3
β-strand	226-229	4	3
α-helix	233-237	5
α-helix	238-243	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Enzyme I	A, B	protein	258	Escherichia coli	P08839 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1ZYM_1 ENZYME I (chains A, B)
MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTK
AGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD
EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFI
TDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR
AVQEQVASEKAELAKLKD

Primary citation

The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr. Liao, D.I., Silverton, E., Seok, Y.J. et al. Structure (1996) 4:861-872. DOI 10.1016/S0969-2126(96)00092-5 · 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…
2HWG 2.7 Å, Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase…
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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