BMRB: 2396

Mapping the Substrate-Binding Site of a Human Class Mu Glutathione Transferase Using Nuclear Magnetic Resonance Spectroscopy

Authors

Penington, C.J., Rule, G.S.

Assembly

glutathione transferase

Entity

1. glutathione transferase (polymer), 218 monomers, 25744.35 Da Detail

MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK

Formula weight

25744.35 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 5.5 %, Completeness: 1.9 %, Completeness (bb): 0.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	1.9 % (27 of 1431)	1.9 % (27 of 1431)
Backbone	0.9 % (4 of 434)	0.9 % (4 of 434)
Sidechain	2.3 % (23 of 997)	2.3 % (23 of 997)
Aromatic	12.2 % (18 of 148)	12.2 % (18 of 148)
Methyl	1.9 % (2 of 105)	1.9 % (2 of 105)

1. glutathione transferase

MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK

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Sample

Temperature 298 K, pH 6.5

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Release date

1995-07-30

Citation

Mapping the substrate-binding site of a human class mu glutathione transferase using nuclear magnetic resonance spectroscopy
Penington, C.J., Rule, G.S.
Biochemistry (1992), 31, 2912-2920, PubMed 1550817 , DOI 10.1021/bi00126a010 , Abstract

Related entities 1. glutathione transferase, : 1 : 2 : 7 : 267 entities Detail

Interaction partners 1. glutathione transferase, : 1 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail