Phosphotransferase

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Template:STRUCTURE 3q2m

Phosphotransferase (PT) are enzymes which catalyze phosphorylation reactions. The acceptor group can be alcohol, carboxy, nitrogenous, phosphate or a pair ofd groups.

Contents

3D structures of phosphotransferase

Updated on 20-August-2014

Phosphotransferase

3our – PT IIA + pyruvate decarboxylase – Vibrio vulnificus
2l5h, 2kx9 - EcPT I - Escherichia coli – NMR
2xdf - EcPT I+ phosphocarrier protein HPR – NMR
3oxp – PT II – Yersinia pestis
3ci6 – PT GAF domain – Acinetobacter
2ooc, 4fpp – PT histidine – Caulobacter crescentus
3ipj – PT IIABC – Clostridium difficile
2f9h - EfPT IIA – Enterococcus faecalis
1c02 - PT - yeast
3n9x – PT – Plasmodium berghei

Aminoglycoside phosphotransferase

3ovc - EcAGPT IA
3r6z, 3uzr - EcAGPT IB
3q2m, 3i1a – LpAGPT IA – Legionella pneumophila
1nd4 – KpAGPT IIA – Klebsiella pneumoniae
1qhn – SvAGPT – Streptomyces venezuelae
3sgc, 3r7z, 3n4t, 3n4u, 3n4v ,4dbx, 4de4 - EncAGPT ID – Enterococcus casseliflavus
1j7i - EfAGPT IIIA

Aminoglycoside phosphotransferase complex with nucleotide

3r70, 4dca - EcAGPT IB + ADP
3r78 - EcAGPT IB + ATP
1qhx - SvAGPT + ATP
3i0q - LpAGPT IA + AMP
1j7l - EfAGPT IIIA + ADP
1j7u - EfAGPT IIIA + AMP-PNP
4ej7 - AGPT IA + ATP – Acinetobacter baumanii
4dt8, 4dt9 - EncAGPT ID + nucleotide
4dta, 4dtb - EncAGPT ID (mutant) + nucleotide

Aminoglycoside phosphotransferase complex with antibiotic

3hav, 3ham - EfAGPT + ATP + antibiotic
3h8p, 3tm0 - EfAGPT + AMP-PNP + antibiotic
2b0q, 1l8t - EfAGPT IIIA + ADP + antibiotic
3r80, 3r81 - EcAGPT ID + antibiotic
1grq, 1grr, 1qhs - SvAGPT + antibiotic
1qhy - SvAGPT + ATPγ + antibiotic
3sg8, 3sg9, 4dfb, 4dfu - EncAGPT ID + antibiotic
3i0o - LpAGPT IA + ADP + antibiotic
4feu, 4fev, 4few, 4fex, 4gkh, 4gki - LpAGPT IA + inhibitor + antibiotic

Aminoglycoside phosphotransferase complex with inhibitor

2bkk, 3q2j - EfAGPT IIIA + inhibitor

Phosphoenolpyruvate-protein phosphotransferase

2xz7 – TtPEP PEP-binding domain + phosphoenolpyruvate – Thermoanaerobacter tengcongensis
2xz9 - TtPEP PEP-binding domain + pyruvate
3nbm – PEP lactose-specific IIBC – Streptococcus pneumoniae
2l2q - PEP cellbiose-specific IIB – Borrelia burgdorferi – NMR
3k1s - PEP cellbiose-specific IIA – Bacillus anthracis
2kyr – EcPEP fructose-specific IIB
2r4q - BsPEP fructose-specific IIABC – Bacillus subtilis
2r48 - BsPEP fructose-specific IIB
1vsq, 2jzh, 2jzn, 2jzo - EcPEP mannose-specific IIA - NMR
3bp3 - EcPEP glucose-specific IIB
1o53 - EcPEP glucose-specific IIA N terminal – NMR
1ggr - EcPEP glucose-specific IIA + phosphocarrier protein HPR – NMR
3bp8 - EcPEP glucose-specific IIB + NAGC-like transcriptional regulator
3eye - EcPEP acetylgalactosamine-specific IIB
2oq3, 1vrv - EcPEP mannitol-specific IIA
1vkr - EcPEP mannitol-specific IIABC – NMR
1j6t - EcPEP mannitol-specific IIABC + phosphocarrier protein HPR – NMR
2few - EcPEP mannitol-specific IIA (mutant)
1wcr - EcPEP diacetylchitobiose-specific IIA (mutant) – NMR
1h9c - EcPEP diacetylchitobiose-specific IIB – NMR
2hwg - EcPEP
3ipr – EfPEP gluconate-specific IIA
3bed - EfPEP mannose-specific IIA
1nrz - KpPEP sorbose-specific IIB
2hro – PEP – Staphylococcus carnosus
2wqd - PEP (mutant) – Staphylococcus aureus
3trc - PEP (mutant) – Coxiella burnetii

1f51, 1pey, 2ftk – BsPT sporulation initiation
1pux - BsPT sporulation initiation – NMR
2jvi, 2jvj, 2jvk - BsPT sporulation initiation (mutant) – NMR
3q15 - BsPT sporulation initiation + response regulator aspartate phosphatase
1fyn – PT SH3 domain + polyproline peptide - human

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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