BMRB: 5054

The Structure of Ap4A Hydrolase Complexed with ATP-MgFx Reveals the Basis of Substrate Binding

Authors

Fletcher, J.I., Swarbrick, J.D., Maksel, D., Gayler, K.R., Gooley, P.R.

Assembly

Diadenosine 5',5'''-P1,P4 tetraphosphate hydrolase complexed with ATP

Entity

1. Ap4A hydrolase (polymer, Thiol state: all free), 165 monomers, 18814.99 Da Detail

GPLGSMDSPP EGYRRNVGIC LMNNDKKIFA ASRLDIPDAW QMPQGGIDEG EDPRNAAIRE LREETGVTSA EVIAEVPYWL TYDFPPKVRE KLNIQWGSDW KGQAQKWFLF KFTGQDQEIN LLGDGSEKPE FGEWSWVTPE QLIDLTVEFK KPVYKEVLSV FAPHL

2. ADENOSINE-5'-TRIPHOSPHATE (non-polymer), 1 monomers, 507.181 Da

Total weight

19322.172 Da

Max. entity weight

18814.99 Da

Source organism

Lupinus angustifolius

Exptl. method

NMR

Refine. method

torsion angle dynamics, simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 98.3 %, Completeness (bb): 98.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	98.3 % (1946 of 1980)	99.2 % (1030 of 1038)	97.3 % (748 of 769)	97.1 % (168 of 173)
Backbone	98.9 % (953 of 964)	98.8 % (327 of 331)	99.2 % (477 of 481)	98.0 % (149 of 152)
Sidechain	97.9 % (1143 of 1167)	99.4 % (703 of 707)	95.9 % (421 of 439)	90.5 % (19 of 21)
Aromatic	91.5 % (183 of 200)	100.0 % (100 of 100)	81.7 % (76 of 93)	100.0 % (7 of 7)
Methyl	100.0 % (158 of 158)	100.0 % (79 of 79)	100.0 % (79 of 79)

1. Ap4A hydrolase

GPLGSMDSPP EGYRRNVGIC LMNNDKKIFA ASRLDIPDAW QMPQGGIDEG EDPRNAAIRE LREETGVTSA EVIAEVPYWL TYDFPPKVRE KLNIQWGSDW KGQAQKWFLF KFTGQDQEIN LLGDGSEKPE FGEWSWVTPE QLIDLTVEFK KPVYKEVLSV FAPHL

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Sample

Temperature 298 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	Ap4A hydrolase	[U-95% 13C; U-95% 15N]		1.6 mM
2	ADENOSINE-5'-TRIPHOSPHATE			1.6 mM
3	Imidazole	[U-100% 2H]		20 mM
4	NaF			32 mM
5	MgCl2			20 mM
6	NaN3			0.02 %

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Chem. Shift Complete2

Sequence coverage: 25.5 %, Completeness: 58.2 %, Completeness (bb): 59.3 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	58.2 % (2306 of 3960)	59.2 % (1229 of 2076)	56.8 % (874 of 1538)	58.7 % (203 of 346)
Backbone	59.3 % (1143 of 1928)	60.6 % (401 of 662)	58.2 % (560 of 962)	59.9 % (182 of 304)
Sidechain	57.6 % (1345 of 2334)	58.6 % (829 of 1414)	56.4 % (495 of 878)	50.0 % (21 of 42)
Aromatic	50.2 % (201 of 400)	54.5 % (109 of 200)	45.7 % (85 of 186)	50.0 % (7 of 14)
Methyl	59.5 % (188 of 316)	60.8 % (96 of 158)	58.2 % (92 of 158)

1. Ap4A hydrolase

GPLGSMDSPP EGYRRNVGIC LMNNDKKIFA ASRLDIPDAW QMPQGGIDEG EDPRNAAIRE LREETGVTSA EVIAEVPYWL TYDFPPKVRE KLNIQWGSDW KGQAQKWFLF KFTGQDQEIN LLGDGSEKPE FGEWSWVTPE QLIDLTVEFK KPVYKEVLSV FAPHL

Show sample condition

Sample

Temperature 298 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	Ap4A hydrolase	[U-95% 13C; U-95% 15N]		1.6 mM
2	ADENOSINE-5'-TRIPHOSPHATE			1.6 mM
3	Imidazole	[U-100% 2H]		20 mM
4	NaF			32 mM
5	MgCl2			20 mM
6	NaN3			0.02 %

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Protein Blocks Logo

Calculated from 30 models in PDB: 1JKN, Strand ID: A Detail

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Release date

2002-04-04

Citation

The structure of Ap(4)A hydrolase complexed with ATP-MgF(x) reveals the basis of substrate binding
Fletcher, J.I., Swarbrick, J.D., Maksel, D., Gayler, K.R., Gooley, P.R.
Structure (2002), 10, 205-213, PubMed 11839306 , DOI: , Abstract

Related entities 1. Ap4A hydrolase, : 1 : 1 : 135 entities Detail

Experiments performed 16 experiments Detail