5UDW
 
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with nickel | | Descriptor: | Lactate racemization operon protein LarE, NICKEL (II) ION, PHOSPHATE ION, ... | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2016-12-28 | | Release date: | 2017-08-23 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (2.698 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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5UDT
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with AMP | | Descriptor: | ADENOSINE MONOPHOSPHATE, Lactate racemization operon protein LarE, PHOSPHATE ION | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2016-12-28 | | Release date: | 2017-08-23 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (3.188 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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5UDX
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with zinc | | Descriptor: | Lactate racemization operon protein LarE, PHOSPHATE ION, SULFATE ION, ... | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2016-12-28 | | Release date: | 2017-08-23 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (2.784 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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5UDQ
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, apo form | | Descriptor: | Lactate racemization operon protein LarE, PHOSPHATE ION, SULFATE ION | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2016-12-28 | | Release date: | 2017-08-23 | | Last modified: | 2024-12-25 | | Method: | X-RAY DIFFRACTION (2.09 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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6DG3
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with caesium | | Descriptor: | CESIUM ION, PHOSPHATE ION, Pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase | | Authors: | Fellner, M, Hausinger, R.P, Hu, J. | | Deposit date: | 2018-05-16 | | Release date: | 2019-05-22 | | Last modified: | 2023-10-11 | | Method: | X-RAY DIFFRACTION (2.944 Å) | | Cite: | Unique cesium-binding sites in proteins, a case study with the sacrificial sulfur transferase LarE
J Life Sci, 2021
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6ECJ
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6UTR
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with copper | | Descriptor: | ATP-dependent sacrificial sulfur transferase LarE, COPPER (II) ION, PHOSPHATE ION, ... | | Authors: | Fellner, M, Huizenga, K, Hausinger, R.P, Hu, J. | | Deposit date: | 2019-10-29 | | Release date: | 2019-11-06 | | Last modified: | 2023-10-11 | | Method: | X-RAY DIFFRACTION (2.41 Å) | | Cite: | Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Sci Rep, 10, 2020
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6UTQ
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with cadmium | | Descriptor: | ATP-dependent sacrificial sulfur transferase LarE, CADMIUM ION, PHOSPHATE ION, ... | | Authors: | Fellner, M, Huizenga, K, Hausinger, R.P, Hu, J. | | Deposit date: | 2019-10-29 | | Release date: | 2019-11-06 | | Last modified: | 2023-10-11 | | Method: | X-RAY DIFFRACTION (2.39 Å) | | Cite: | Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Sci Rep, 10, 2020
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6UTT
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with calcium | | Descriptor: | ATP-dependent sacrificial sulfur transferase LarE, CALCIUM ION, PHOSPHATE ION, ... | | Authors: | Fellner, M, Huizenga, K, Hausinger, R.P, Hu, J. | | Deposit date: | 2019-10-29 | | Release date: | 2019-11-06 | | Last modified: | 2023-10-11 | | Method: | X-RAY DIFFRACTION (2.49 Å) | | Cite: | Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Sci Rep, 10, 2020
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6UTP
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with cobalt | | Descriptor: | ATP-dependent sacrificial sulfur transferase LarE, COBALT (II) ION, PHOSPHATE ION, ... | | Authors: | Fellner, M, Huizenga, K, Hausinger, R.P, Hu, J. | | Deposit date: | 2019-10-29 | | Release date: | 2019-11-06 | | Last modified: | 2023-10-11 | | Method: | X-RAY DIFFRACTION (3.55 Å) | | Cite: | Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Sci Rep, 10, 2020
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5UDV
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with iron | | Descriptor: | FE (III) ION, Lactate racemization operon protein LarE, PHOSPHATE ION, ... | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2016-12-28 | | Release date: | 2017-08-23 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (2.621 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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5UDR
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with nicotinamide mononucleotid NMN | | Descriptor: | ATP-utilizing enzyme of the PP-loopsuperfamily, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE, MANGANESE (II) ION | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2016-12-28 | | Release date: | 2017-08-23 | | Last modified: | 2024-03-06 | | Method: | X-RAY DIFFRACTION (2.62 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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5UDU
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with manganese | | Descriptor: | Lactate racemization operon protein LarE, MANGANESE (II) ION, PHOSPHATE ION, ... | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2016-12-28 | | Release date: | 2017-08-23 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (2.792 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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5UDS
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with MgATP | | Descriptor: | ADENOSINE-5'-TRIPHOSPHATE, Lactate racemization operon protein LarE, MAGNESIUM ION, ... | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2016-12-28 | | Release date: | 2017-08-23 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (2.37 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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5UNM
 | | LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, substrate free form with flexible loop | | Descriptor: | ATP-utilizing enzyme of the PP-loopsuperfamily, PHOSPHATE ION | | Authors: | Fellner, M, Desguin, B, Hausinger, R.P, Hu, J. | | Deposit date: | 2017-01-31 | | Release date: | 2017-08-23 | | Last modified: | 2024-03-06 | | Method: | X-RAY DIFFRACTION (2.58 Å) | | Cite: | Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114, 2017
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9BNQ
 | | N-(4-(isothiocyanatomethyl)phenyl)methanesulfonamide complexed with Macrophage Migration Inhibitory Factor | | Descriptor: | ISOPROPYL ALCOHOL, Macrophage migration inhibitory factor, N-{[4-(methanesulfonamido)phenyl]methyl}methanethioamide, ... | | Authors: | Fellner, M, Rutledge, M.T, Putha, L, Kok, L.K, Gamble, A.B, Wilbanks, S.M, Vernall, A.J, Tyndall, J.D.A. | | Deposit date: | 2024-05-02 | | Release date: | 2024-07-24 | | Last modified: | 2024-11-20 | | Method: | X-RAY DIFFRACTION (1.09 Å) | | Cite: | Covalent Isothiocyanate Inhibitors of Macrophage Migration Inhibitory Factor as Potential Colorectal Cancer Treatments.
Chemmedchem, 19, 2024
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9BNR
 | | 4-(2-isothiocyanatoethyl)benzenesulfonamide complexed with Macrophage Migration Inhibitory Factor | | Descriptor: | Macrophage migration inhibitory factor, N-[2-(4-sulfamoylphenyl)ethyl]methanethioamide, SULFATE ION | | Authors: | Fellner, M, Rutledge, M.T, Putha, L, Kok, L.K, Gamble, A.B, Wilbanks, S.M, Vernall, A.J, Tyndall, J.D.A. | | Deposit date: | 2024-05-02 | | Release date: | 2024-07-24 | | Last modified: | 2024-11-20 | | Method: | X-RAY DIFFRACTION (1.53 Å) | | Cite: | Covalent Isothiocyanate Inhibitors of Macrophage Migration Inhibitory Factor as Potential Colorectal Cancer Treatments.
Chemmedchem, 19, 2024
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4UBG
 | | Resting state of rat cysteine dioxygenase C93G variant | | Descriptor: | Cysteine dioxygenase type 1, FE (II) ION, SODIUM ION | | Authors: | Fellner, M, Tchesnokov, E.P, Jameson, G.N, Wilbanks, S.M. | | Deposit date: | 2014-08-13 | | Release date: | 2014-11-26 | | Last modified: | 2023-09-27 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | The Cys-Tyr Cross-Link of Cysteine Dioxygenase Changes the Optimal pH of the Reaction without a Structural Change.
Biochemistry, 53, 2014
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8UGM
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8UIX
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8UWM
 | | FphE, Staphylococcus aureus fluorophosphonate-binding serine hydrolases E, borolane-based compound Q41 bound | | Descriptor: | 2-methyl-4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)benzene-1-sulfonamide, CALCIUM ION, Fluorophosphonate-binding serine hydrolase E | | Authors: | Fellner, M. | | Deposit date: | 2023-11-06 | | Release date: | 2024-11-20 | | Last modified: | 2025-06-25 | | Method: | X-RAY DIFFRACTION (1.97 Å) | | Cite: | Identification of covalent inhibitors of Staphylococcus aureus serine hydrolases important for virulence and biofilm formation.
Nat Commun, 16, 2025
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4TLF
 | | Crystal structure of Thiol dioxygenase from Pseudomonas aeruginosa | | Descriptor: | 3-mercaptopropionate dioxygenase, FE (II) ION | | Authors: | Fellner, M, Tchesnokov, E.P, Jameson, G.N.L, Wilbanks, S.M. | | Deposit date: | 2014-05-29 | | Release date: | 2015-06-17 | | Last modified: | 2023-09-27 | | Method: | X-RAY DIFFRACTION (2.137 Å) | | Cite: | The Cysteine Dioxygenase Homologue from Pseudomonas aeruginosa Is a 3-Mercaptopropionate Dioxygenase.
J.Biol.Chem., 290, 2015
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9DRO
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6OC5
 | | Lanthanide-dependent methanol dehydrogenase XoxF from Methylobacterium extorquens, in complex with Lanthanum | | Descriptor: | LANTHANUM (III) ION, Lanthanide-dependent methanol dehydrogenase XoxF | | Authors: | Fellner, M, Good, N.M, Martinez-Gomez, N.C, Hausinger, R.P, Hu, J. | | Deposit date: | 2019-03-21 | | Release date: | 2020-05-13 | | Last modified: | 2024-11-13 | | Method: | X-RAY DIFFRACTION (2.8 Å) | | Cite: | Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function.
J.Biol.Chem., 295, 2020
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6OC6
 | | Lanthanide-dependent methanol dehydrogenase XoxF from Methylobacterium extorquens, in complex with Lanthanum and Pyrroloquinoline quinone | | Descriptor: | LANTHANUM (III) ION, Lanthanide-dependent methanol dehydrogenase XoxF, PYRROLOQUINOLINE QUINONE | | Authors: | Fellner, M, Good, N.M, Martinez-Gomez, N.C, Hausinger, R.P, Hu, J. | | Deposit date: | 2019-03-21 | | Release date: | 2020-05-13 | | Last modified: | 2024-10-16 | | Method: | X-RAY DIFFRACTION (2.89 Å) | | Cite: | Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function.
J.Biol.Chem., 295, 2020
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