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6v8d

Design, Synthesis, and Mechanism of Fluorine-substituted Cyclohexene Analogues of GAMA-Aminobutyric Acid (GABA) as Selective Ornithine Aminotransferase Inactivators

Method: X-RAY DIFFRACTION Dmax: 117.8 Å Quality: GOOD
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1. 蛋白身份与相关结构 Protein Identity & Related Structures

Ornithine aminotransferase, mitochondrial

Homo sapiens

UniProt P04181

当前结构中的状态

Assembly 聚集状态 构建体 突变与修饰 配体、离子与共同组分 实验方法与环境 结构质量
1 蛋白同源多聚体 同源多聚体 蛋白 × 2 PDB 声明：dimeric（2） 与蛋白拷贝数一致 链 A； UniProt 36–439 链 B； UniProt 36–439 未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 O78 (3Z)-3-iminocyclohex-1-ene-1-carboxylic acid × 2 X-RAY DIFFRACTION X-ray结晶条件：VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；16.5% PEG 1000 240 mM NaCl 25% glycerol 50 mM Tricine pH 7.8 分辨率 2.25 Å R-free 0.196
2 蛋白同源多聚体 同源多聚体 蛋白 × 2 PDB 声明：dimeric（2） 与蛋白拷贝数一致 链 C； UniProt 36–439 未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 O78 (3Z)-3-iminocyclohex-1-ene-1-carboxylic acid × 2 X-RAY DIFFRACTION X-ray结晶条件：VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；16.5% PEG 1000 240 mM NaCl 25% glycerol 50 mM Tricine pH 7.8 分辨率 2.25 Å R-free 0.196

数据库中的同蛋白其他状态

以下每一行都是同一 UniProt 蛋白在另一个 PDB 条目中的 biological assembly， “相对当前条目”直接指出证据层面的不同；没有差异标签表示当前已读取字段一致。

其他 PDB 相对当前条目 6V8D Assembly / 聚集状态 构建体 突变与修饰 配体、离子与非聚合物 实验方法与环境 结构质量
10LW Final Adduct of Human Ornithine Aminotransferase Inactivated by (1R,4S)-4-Amino-3-(trifluoromethyl)cyclopent-2-ene-1-carboxylic Acid 提交 2026-01-27 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 1–439（439 aa）
未记录 RMT (3R,4E)-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]cyclopent-1-ene-1,3-dicarboxylic acid × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；7.25%-8.50% PEG 6000, 100 mM-250 mM NaCl, 2-3.5% glycerol, and 100 mM Tricine pH 7.8.
分辨率 1.93 Å R-free 0.217
10LW Final Adduct of Human Ornithine Aminotransferase Inactivated by (1R,4S)-4-Amino-3-(trifluoromethyl)cyclopent-2-ene-1-carboxylic Acid 提交 2026-01-27 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 1–439（439 aa）
链 C 1–439（439 aa）
未记录 RMT (3R,4E)-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]cyclopent-1-ene-1,3-dicarboxylic acid × 2 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；7.25%-8.50% PEG 6000, 100 mM-250 mM NaCl, 2-3.5% glycerol, and 100 mM Tricine pH 7.8.
分辨率 1.93 Å R-free 0.217
10LX High Stable Quinonoid Intermediate of Human Ornithine Aminotransferase Complexed with (1R,4S)-4-Amino-3-(trifluoromethyl)cyclopent-2-ene-1-carboxylic Acid 提交 2026-01-27 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 1–439（439 aa）
链 C 1–439（439 aa）
未记录 A1C6V (1S,4R)-4-(difluoromethyl)-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopent-2-ene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；298 K；7.25%-8.50% PEG 6000, 100 mM-250 mM NaCl, 2-3.5% glycerol, and 100 mM Tricine pH 7.8.
分辨率 1.83 Å R-free 0.234
10LX High Stable Quinonoid Intermediate of Human Ornithine Aminotransferase Complexed with (1R,4S)-4-Amino-3-(trifluoromethyl)cyclopent-2-ene-1-carboxylic Acid 提交 2026-01-27 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 1–439（439 aa）
未记录 A1C6V (1S,4R)-4-(difluoromethyl)-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopent-2-ene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；298 K；7.25%-8.50% PEG 6000, 100 mM-250 mM NaCl, 2-3.5% glycerol, and 100 mM Tricine pH 7.8.
分辨率 1.83 Å R-free 0.234
1GBN HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH THE NEUROTOXIN GABACULINE 提交 1997-05-29 构建体不同 突变/修饰不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 3 PDB 声明：trimeric
链 A 38–439（402 aa）
链 B 38–439（402 aa）
链 C 38–439（402 aa）
未记录 GAB 3-AMINOBENZOIC ACID × 1 PLP PYRIDOXAL-5'-PHOSPHATE × 3 GBC GABACULINE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 6.5；pH 6.5
分辨率 2.30 Å R-free 0.235
1GBN HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH THE NEUROTOXIN GABACULINE 提交 1997-05-29 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 38–439（402 aa）
链 B 38–439（402 aa）
未记录 GAB 3-AMINOBENZOIC ACID × 1 PLP PYRIDOXAL-5'-PHOSPHATE × 2 GBC GABACULINE × 1 X-RAY DIFFRACTION
X-ray结晶条件 pH 6.5；pH 6.5
分辨率 2.30 Å R-free 0.235
1GBN HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH THE NEUROTOXIN GABACULINE 提交 1997-05-29 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 38–439（402 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 GBC GABACULINE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 6.5；pH 6.5
分辨率 2.30 Å R-free 0.235
1GBN HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH THE NEUROTOXIN GABACULINE 提交 1997-05-29 构建体不同 突变/修饰不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 4 蛋白同源多聚体 同源多聚体；蛋白 × 4 PDB 声明：tetrameric
链 A 38–439（402 aa）
链 B 38–439（402 aa）
链 C 38–439（402 aa）
未记录 GAB 3-AMINOBENZOIC ACID × 1 PLP PYRIDOXAL-5'-PHOSPHATE × 4 GBC GABACULINE × 3 X-RAY DIFFRACTION
X-ray结晶条件 pH 6.5；pH 6.5
分辨率 2.30 Å R-free 0.235
1OAT ORNITHINE AMINOTRANSFERASE 提交 1997-03-26 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 1–439（439 aa）
链 B 1–439（439 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.8；pH 7.8
分辨率 2.50 Å R-free 0.235
1OAT ORNITHINE AMINOTRANSFERASE 提交 1997-03-26 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 1–439（439 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.8；pH 7.8
分辨率 2.50 Å R-free 0.235
2BYJ Ornithine aminotransferase mutant Y85I 提交 2005-08-02 构建体不同 突变/修饰不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 1–439（439 aa）
链 B 1–439（439 aa）
突变：YES 突变：YES PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.9；6-10%PEG6000, 120-160MM NACL, 50MM TRICINE PH7.9, 1MM DTT, pH 7.90
分辨率 3.02 Å R-free 0.226
2BYJ Ornithine aminotransferase mutant Y85I 提交 2005-08-02 构建体不同 突变/修饰不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 1–439（439 aa）
突变：YES PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.9；6-10%PEG6000, 120-160MM NACL, 50MM TRICINE PH7.9, 1MM DTT, pH 7.90
分辨率 3.02 Å R-free 0.226
2BYL Structure of ornithine aminotransferase triple mutant Y85I Y55A G320F 提交 2005-08-03 构建体不同 突变/修饰不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 1–439（439 aa）
链 B 1–439（439 aa）
突变：YES 突变：YES PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.9；6-10%PEG6000, 120-160MM NACL, 50MM TRICINE PH7.9, 1MM DTT, pH 7.90
分辨率 2.15 Å R-free 0.191
2BYL Structure of ornithine aminotransferase triple mutant Y85I Y55A G320F 提交 2005-08-03 构建体不同 突变/修饰不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 1–439（439 aa）
突变：YES PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.9；6-10%PEG6000, 120-160MM NACL, 50MM TRICINE PH7.9, 1MM DTT, pH 7.90
分辨率 2.15 Å R-free 0.191
2CAN HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH L-CANALINE 提交 1997-05-29 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 38–439（402 aa）
链 B 38–439（402 aa）
未记录 CAN CANALINE × 2 PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 6.5；pH 6.5
分辨率 2.30 Å R-free 0.238
2CAN HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH L-CANALINE 提交 1997-05-29 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 38–439（402 aa）
未记录 CAN CANALINE × 2 PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 6.5；pH 6.5
分辨率 2.30 Å R-free 0.238
2OAT ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE 提交 1998-05-07 构建体不同 突变/修饰不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 4 PDB 声明：tetrameric
链 A 1–439（439 aa）
链 B 1–439（439 aa）
链 C 1–439（439 aa）
未记录 PFM 1-AMINO-7-(2-METHYL-3-OXIDO-5-((PHOSPHONOXY)METHYL)-4-PYRIDOXAL-5-OXO-6-HEPTENATE × 4 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.9；(2S,5S)5FMORN-OAT WAS CO-CRYSTALLIZED FROM 6-10% PEG 6000, 1MM DTT, 120-160 MM NACL, 10-20% GLYCEROL, 50 MM TRICIN, PH 7.9.
分辨率 1.95 Å R-free 0.232
2OAT ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE 提交 1998-05-07 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 1–439（439 aa）
链 B 1–439（439 aa）
未记录 PFM 1-AMINO-7-(2-METHYL-3-OXIDO-5-((PHOSPHONOXY)METHYL)-4-PYRIDOXAL-5-OXO-6-HEPTENATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.9；(2S,5S)5FMORN-OAT WAS CO-CRYSTALLIZED FROM 6-10% PEG 6000, 1MM DTT, 120-160 MM NACL, 10-20% GLYCEROL, 50 MM TRICIN, PH 7.9.
分辨率 1.95 Å R-free 0.232
2OAT ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE 提交 1998-05-07 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 1–439（439 aa）
未记录 PFM 1-AMINO-7-(2-METHYL-3-OXIDO-5-((PHOSPHONOXY)METHYL)-4-PYRIDOXAL-5-OXO-6-HEPTENATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 pH 7.9；(2S,5S)5FMORN-OAT WAS CO-CRYSTALLIZED FROM 6-10% PEG 6000, 1MM DTT, 120-160 MM NACL, 10-20% GLYCEROL, 50 MM TRICIN, PH 7.9.
分辨率 1.95 Å R-free 0.232
5VWO Ornithine aminotransferase inactivated by (1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP) 提交 2017-05-22 构建体不同 突变/修饰不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 3 PDB 声明：trimeric
链 A 36–439（404 aa） 片段：UNP residues 36-439
链 B 36–439（404 aa） 片段：UNP residues 36-439
链 C 36–439（404 aa） 片段：UNP residues 36-439
未记录 9QJ (1S,3S,4E)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid × 3 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；298 K；NaCl (175mM), 8-10% (v/v) PEG 6000
分辨率 1.77 Å R-free 0.210
6HX7 Crystal structure of human R180T variant of ORNITHINE AMINOTRANSFERASE at 1.8 Angstrom 提交 2018-10-16 构建体不同 突变/修饰不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 26–439（414 aa）
突变：R180T, A25M PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 7；294 K；Prot 115uM in 150mM NaCl 50mM Hepes pH 8.0 mixed with hit 1-5 of the LMB screen (Molecular Dimensions): 4 M Ammonium acetate 0.1 M Bis-Tris propane 7.0 (cryo + Glycerol 20%)
分辨率 1.80 Å R-free 0.228
6HX7 Crystal structure of human R180T variant of ORNITHINE AMINOTRANSFERASE at 1.8 Angstrom 提交 2018-10-16 构建体不同 突变/修饰不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 26–439（414 aa）
突变：R180T, A25M PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 7；294 K；Prot 115uM in 150mM NaCl 50mM Hepes pH 8.0 mixed with hit 1-5 of the LMB screen (Molecular Dimensions): 4 M Ammonium acetate 0.1 M Bis-Tris propane 7.0 (cryo + Glycerol 20%)
分辨率 1.80 Å R-free 0.228
6HX7 Crystal structure of human R180T variant of ORNITHINE AMINOTRANSFERASE at 1.8 Angstrom 提交 2018-10-16 构建体不同 突变/修饰不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 26–439（414 aa）
突变：R180T, A25M PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 7；294 K；Prot 115uM in 150mM NaCl 50mM Hepes pH 8.0 mixed with hit 1-5 of the LMB screen (Molecular Dimensions): 4 M Ammonium acetate 0.1 M Bis-Tris propane 7.0 (cryo + Glycerol 20%)
分辨率 1.80 Å R-free 0.228
6OIA (1S,3S)-3-amino-4-(perfluoropropan-2-ylidene)cyclopentane-1-carboxylic acid hydrochloride, a potent inhibitor of ornithine aminotransferase 提交 2019-04-09 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
链 B 36–439（404 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 GOL GLYCEROL × 2 MQ4 (1S)-3-amino-4-[(2S)-1,1,1-trifluoro-3-oxopropan-2-yl]cyclopent-3-ene-1-carboxylic acid × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；298 K；10% PEG 6000, 200 mM NaCl, 2.5 % Glycerol
分辨率 1.78 Å R-free 0.189
6OIA (1S,3S)-3-amino-4-(perfluoropropan-2-ylidene)cyclopentane-1-carboxylic acid hydrochloride, a potent inhibitor of ornithine aminotransferase 提交 2019-04-09 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 36–439（404 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 MQ4 (1S)-3-amino-4-[(2S)-1,1,1-trifluoro-3-oxopropan-2-yl]cyclopent-3-ene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；298 K；10% PEG 6000, 200 mM NaCl, 2.5 % Glycerol
分辨率 1.78 Å R-free 0.189
6V8C Design, Synthesis, and Mechanism of Fluorine-substituted Cyclohexene Analogues of GAMA-Aminobutyric Acid (GABA) as Selective Ornithine Aminotransferase Inactivators 提交 2019-12-10 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 QRM 3-aminocyclohexa-1,3-diene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；16.5% PEG 1000 240 mM NaCl 25% glycerol.
分辨率 1.90 Å R-free 0.268
6V8C Design, Synthesis, and Mechanism of Fluorine-substituted Cyclohexene Analogues of GAMA-Aminobutyric Acid (GABA) as Selective Ornithine Aminotransferase Inactivators 提交 2019-12-10 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 QRM 3-aminocyclohexa-1,3-diene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；16.5% PEG 1000 240 mM NaCl 25% glycerol.
分辨率 1.90 Å R-free 0.268
6V8C Design, Synthesis, and Mechanism of Fluorine-substituted Cyclohexene Analogues of GAMA-Aminobutyric Acid (GABA) as Selective Ornithine Aminotransferase Inactivators 提交 2019-12-10 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 36–439（404 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 QRM 3-aminocyclohexa-1,3-diene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；16.5% PEG 1000 240 mM NaCl 25% glycerol.
分辨率 1.90 Å R-free 0.268
7JX9 The crystal structure of human ornithine aminotransferase with an intermediate bound during inactivation by (1S,3S)-3-amino-4-(hexafluoropropan-2-ylidenyl)-cyclopentane-1-carboxylic acid. 提交 2020-08-26 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 IF1 (1S,3S,4S)-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-(1,1,3,3,3-pentafluoroprop-1-en-2-yl)cyclopentane-1-carboxylic acid × 2 VLS N-[1,3-dihydroxy-2-(hydroxymethyl)propan-2-yl]glycine × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；290 K；10% PEG 6000, 100 mM NaCl, and 10% glycerol, Tricine 100 mM, pH 7.8
分辨率 1.96 Å R-free 0.213
7JX9 The crystal structure of human ornithine aminotransferase with an intermediate bound during inactivation by (1S,3S)-3-amino-4-(hexafluoropropan-2-ylidenyl)-cyclopentane-1-carboxylic acid. 提交 2020-08-26 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
链 C 36–439（404 aa）
未记录 IF1 (1S,3S,4S)-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-(1,1,3,3,3-pentafluoroprop-1-en-2-yl)cyclopentane-1-carboxylic acid × 2 VLS N-[1,3-dihydroxy-2-(hydroxymethyl)propan-2-yl]glycine × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；290 K；10% PEG 6000, 100 mM NaCl, and 10% glycerol, Tricine 100 mM, pH 7.8
分辨率 1.96 Å R-free 0.213
7LK0 Ornithine Aminotransferase (OAT) cocrystallized with its potent inhibitor - (S)-3-amino-4,4-difluorocyclopent-1-enecarboxylic acid (SS-1-148) 提交 2021-02-01 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 Y3D (1R,3S)-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-oxocyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；OAT was buffer exchanged into crystallization buffer (50 mM Tricine pH 7.8) supplied with 1 mM 2-ketoglutarate. Then the protein was concentrated to 6 mg/mL. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of 10 mM SS-1-148. The crystals with the best morphology and size grew in a final condition containing 10% PEG 6000, 200 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8.
分辨率 1.96 Å R-free 0.268
7LK0 Ornithine Aminotransferase (OAT) cocrystallized with its potent inhibitor - (S)-3-amino-4,4-difluorocyclopent-1-enecarboxylic acid (SS-1-148) 提交 2021-02-01 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
未记录 Y3D (1R,3S)-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-oxocyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；OAT was buffer exchanged into crystallization buffer (50 mM Tricine pH 7.8) supplied with 1 mM 2-ketoglutarate. Then the protein was concentrated to 6 mg/mL. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of 10 mM SS-1-148. The crystals with the best morphology and size grew in a final condition containing 10% PEG 6000, 200 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8.
分辨率 1.96 Å R-free 0.268
7LK0 Ornithine Aminotransferase (OAT) cocrystallized with its potent inhibitor - (S)-3-amino-4,4-difluorocyclopent-1-enecarboxylic acid (SS-1-148) 提交 2021-02-01 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 36–439（404 aa）
未记录 Y3D (1R,3S)-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-oxocyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；OAT was buffer exchanged into crystallization buffer (50 mM Tricine pH 7.8) supplied with 1 mM 2-ketoglutarate. Then the protein was concentrated to 6 mg/mL. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of 10 mM SS-1-148. The crystals with the best morphology and size grew in a final condition containing 10% PEG 6000, 200 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8.
分辨率 1.96 Å R-free 0.268
7LK1 Ornithine Aminotransferase (OAT) with its potent inhibitor - (S)-3-amino-4,4-difluorocyclopent-1-enecarboxylic acid (SS-1-148) - 1 Hour Soaking 提交 2021-02-01 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 Y37 (1R,4R)-4-fluoro-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopent-2-ene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 10% PEG 6000, 200 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8. Once the holoenzyme crystals reached their maximum size, 2 uL of 16 mM SS-1-148 was added to the drop with crystals. The crystals were soaked for 1 h, transferred into cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 1.79 Å R-free 0.241
7LK1 Ornithine Aminotransferase (OAT) with its potent inhibitor - (S)-3-amino-4,4-difluorocyclopent-1-enecarboxylic acid (SS-1-148) - 1 Hour Soaking 提交 2021-02-01 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
链 C 36–439（404 aa）
未记录 Y37 (1R,4R)-4-fluoro-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopent-2-ene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 10% PEG 6000, 200 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8. Once the holoenzyme crystals reached their maximum size, 2 uL of 16 mM SS-1-148 was added to the drop with crystals. The crystals were soaked for 1 h, transferred into cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 1.79 Å R-free 0.241
7LNM Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclopentene-1-carboxylic acid 提交 2021-02-07 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
链 C 36–439（404 aa）
未记录 Y7S (1~{R},3~{S},4~{R})-3-methyl-4-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The freshly prepared enzyme was buffer exchanged into 50 mM Tricine pH 7.8 and concentrated to a protein concentration of 6 mg/mL. For each hanging drop, 2 ul of protein solution was mixed with equal volume of well solution and 0.5 ul of 10 mM compound. The crystals with the best morphology and size grew in a final condition containing 12% PEG 8000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8.
分辨率 2.00 Å R-free 0.186
7LNM Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclopentene-1-carboxylic acid 提交 2021-02-07 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 E 36–439（404 aa）
链 F 36–439（404 aa）
未记录 Y7S (1~{R},3~{S},4~{R})-3-methyl-4-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The freshly prepared enzyme was buffer exchanged into 50 mM Tricine pH 7.8 and concentrated to a protein concentration of 6 mg/mL. For each hanging drop, 2 ul of protein solution was mixed with equal volume of well solution and 0.5 ul of 10 mM compound. The crystals with the best morphology and size grew in a final condition containing 12% PEG 8000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8.
分辨率 2.00 Å R-free 0.186
7LNM Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclopentene-1-carboxylic acid 提交 2021-02-07 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 I 36–439（404 aa）
链 J 36–439（404 aa）
未记录 Y7S (1~{R},3~{S},4~{R})-3-methyl-4-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The freshly prepared enzyme was buffer exchanged into 50 mM Tricine pH 7.8 and concentrated to a protein concentration of 6 mg/mL. For each hanging drop, 2 ul of protein solution was mixed with equal volume of well solution and 0.5 ul of 10 mM compound. The crystals with the best morphology and size grew in a final condition containing 12% PEG 8000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8.
分辨率 2.00 Å R-free 0.186
7LOM Ornithine Aminotransferase (OAT) soaked with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid 提交 2021-02-10 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 THR THREONINE × 2 Y8P (3~{S},4~{S})-4-methyl-3-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclohexene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once the holoenzyme crystals reached their maximum size within five days, 1 uL of 10 mM 181 was added to the drop with crystals. Within the first three minutes of 181 addition, the hOAT crystals turned their color from yellow to transparent. The crystals were soaked for 44 minutes, transferred into cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.10 Å R-free 0.235
7LOM Ornithine Aminotransferase (OAT) soaked with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid 提交 2021-02-10 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
链 C 36–439（404 aa）
未记录 THR THREONINE × 2 Y8P (3~{S},4~{S})-4-methyl-3-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclohexene-1-carboxylic acid × 1 YCD (4~{R})-4-(fluoranylmethyl)-3-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclohexene-1-carboxylic acid × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once the holoenzyme crystals reached their maximum size within five days, 1 uL of 10 mM 181 was added to the drop with crystals. Within the first three minutes of 181 addition, the hOAT crystals turned their color from yellow to transparent. The crystals were soaked for 44 minutes, transferred into cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.10 Å R-free 0.235
7LON Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid 提交 2021-02-10 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
未记录 THR THREONINE × 2 7QP (1R,3S,4R)-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-methylcyclohexane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The freshly prepared enzyme was buffer exchanged into 50 mM Tricine pH 7.8 and concentrated to a protein concentration of 6 mg/mL. For each hanging drop, 2 ul of protein solution was mixed with equal volume of well solution and 0.5 ul of 10 mM compound. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8.
分辨率 1.95 Å R-free 0.278
7LON Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid 提交 2021-02-10 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 THR THREONINE × 2 7QP (1R,3S,4R)-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-methylcyclohexane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The freshly prepared enzyme was buffer exchanged into 50 mM Tricine pH 7.8 and concentrated to a protein concentration of 6 mg/mL. For each hanging drop, 2 ul of protein solution was mixed with equal volume of well solution and 0.5 ul of 10 mM compound. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8.
分辨率 1.95 Å R-free 0.278
7LON Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid 提交 2021-02-10 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 36–439（404 aa）
未记录 THR THREONINE × 2 7QP (1R,3S,4R)-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-methylcyclohexane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The freshly prepared enzyme was buffer exchanged into 50 mM Tricine pH 7.8 and concentrated to a protein concentration of 6 mg/mL. For each hanging drop, 2 ul of protein solution was mixed with equal volume of well solution and 0.5 ul of 10 mM compound. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8.
分辨率 1.95 Å R-free 0.278
7T9Z Human Ornithine Aminotransferase (hOAT) crystallized at pH 6.0 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 A 1–439（439 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；Purified holo-hOAT was buffer-exchanged into 100 mM MES, 200 mM NaCl, 100 uM PLP, pH 6.0 buffer, and then concentrated to ~6 mg/mL. The crystallization was performed via the hanging drop vapor diffusion method according to previously published conditions with 50 mM Tricine pH 7.8 substituted to 50 mM MES pH 6.0 buffer. The crystals grew at room temperature within three days and reached their maximum size in a week.
分辨率 2.15 Å R-free 0.276
7T9Z Human Ornithine Aminotransferase (hOAT) crystallized at pH 6.0 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 B 1–439（439 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；Purified holo-hOAT was buffer-exchanged into 100 mM MES, 200 mM NaCl, 100 uM PLP, pH 6.0 buffer, and then concentrated to ~6 mg/mL. The crystallization was performed via the hanging drop vapor diffusion method according to previously published conditions with 50 mM Tricine pH 7.8 substituted to 50 mM MES pH 6.0 buffer. The crystals grew at room temperature within three days and reached their maximum size in a week.
分辨率 2.15 Å R-free 0.276
7T9Z Human Ornithine Aminotransferase (hOAT) crystallized at pH 6.0 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 C 1–439（439 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；Purified holo-hOAT was buffer-exchanged into 100 mM MES, 200 mM NaCl, 100 uM PLP, pH 6.0 buffer, and then concentrated to ~6 mg/mL. The crystallization was performed via the hanging drop vapor diffusion method according to previously published conditions with 50 mM Tricine pH 7.8 substituted to 50 mM MES pH 6.0 buffer. The crystals grew at room temperature within three days and reached their maximum size in a week.
分辨率 2.15 Å R-free 0.276
7TA0 Human Ornithine Aminotransferase (hOAT) soaked with 5-aminovaleric acid 提交 2021-12-20 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 1–439（439 aa）
链 B 1–439（439 aa）
未记录 I3B 5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid × 2 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；Once hOAT was purified, it was transferred to a 10 kDa centrifugal filter tube and concentrated to ~6 mg/mL. The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once holoenzyme crystals reached their maximum size within seven days, 1 uL of 5-aminovaleric acid was added to the drop with crystals. The crystals were soaked for different time periods from 3 to 59 minutes. After soaking, crystals were transferred into a cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.33 Å R-free 0.236
7TA0 Human Ornithine Aminotransferase (hOAT) soaked with 5-aminovaleric acid 提交 2021-12-20 构建体不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 1–439（439 aa）
未记录 I3B 5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；Once hOAT was purified, it was transferred to a 10 kDa centrifugal filter tube and concentrated to ~6 mg/mL. The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once holoenzyme crystals reached their maximum size within seven days, 1 uL of 5-aminovaleric acid was added to the drop with crystals. The crystals were soaked for different time periods from 3 to 59 minutes. After soaking, crystals were transferred into a cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.33 Å R-free 0.236
7TA1 Human Ornithine Aminotransferase (hOAT) soaked with gamma-Aminobutyric acid 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 A 1–439（439 aa）
未记录 PLZ 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]BUTANOIC ACID × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；Once hOAT was purified, it was transferred to a 10 kDa centrifugal filter tube and concentrated to ~6 mg/mL. The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once holoenzyme crystals reached their maximum size within seven days, 1 uL of 10 mM GABA was added to the drop with crystals. The crystals were soaked for different time periods from 50 minutes to 2.5 hours. After soaking, crystals were transferred into a cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.20 Å R-free 0.268
7TA1 Human Ornithine Aminotransferase (hOAT) soaked with gamma-Aminobutyric acid 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 B 1–439（439 aa）
未记录 PLZ 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]BUTANOIC ACID × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；Once hOAT was purified, it was transferred to a 10 kDa centrifugal filter tube and concentrated to ~6 mg/mL. The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once holoenzyme crystals reached their maximum size within seven days, 1 uL of 10 mM GABA was added to the drop with crystals. The crystals were soaked for different time periods from 50 minutes to 2.5 hours. After soaking, crystals were transferred into a cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.20 Å R-free 0.268
7TA1 Human Ornithine Aminotransferase (hOAT) soaked with gamma-Aminobutyric acid 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 C 1–439（439 aa）
未记录 PLZ 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]BUTANOIC ACID × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；Once hOAT was purified, it was transferred to a 10 kDa centrifugal filter tube and concentrated to ~6 mg/mL. The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once holoenzyme crystals reached their maximum size within seven days, 1 uL of 10 mM GABA was added to the drop with crystals. The crystals were soaked for different time periods from 50 minutes to 2.5 hours. After soaking, crystals were transferred into a cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.20 Å R-free 0.268
7TA1 Human Ornithine Aminotransferase (hOAT) soaked with gamma-Aminobutyric acid 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 4 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 D 1–439（439 aa）
未记录 PLZ 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]BUTANOIC ACID × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；Once hOAT was purified, it was transferred to a 10 kDa centrifugal filter tube and concentrated to ~6 mg/mL. The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once holoenzyme crystals reached their maximum size within seven days, 1 uL of 10 mM GABA was added to the drop with crystals. The crystals were soaked for different time periods from 50 minutes to 2.5 hours. After soaking, crystals were transferred into a cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.20 Å R-free 0.268
7TA1 Human Ornithine Aminotransferase (hOAT) soaked with gamma-Aminobutyric acid 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 5 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 E 1–439（439 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；Once hOAT was purified, it was transferred to a 10 kDa centrifugal filter tube and concentrated to ~6 mg/mL. The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once holoenzyme crystals reached their maximum size within seven days, 1 uL of 10 mM GABA was added to the drop with crystals. The crystals were soaked for different time periods from 50 minutes to 2.5 hours. After soaking, crystals were transferred into a cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.20 Å R-free 0.268
7TA1 Human Ornithine Aminotransferase (hOAT) soaked with gamma-Aminobutyric acid 提交 2021-12-20 构建体不同 聚集状态不同 配体/离子不同 实验环境不同 结构质量不同 Assembly 6 蛋白单体 单体；蛋白 × 1 PDB 声明：monomeric
链 F 1–439（439 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；Once hOAT was purified, it was transferred to a 10 kDa centrifugal filter tube and concentrated to ~6 mg/mL. The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 8% PEG 6000, 100 mM NaCl, 5% glycerol, and 50 mM Tricine pH 7.8. Once holoenzyme crystals reached their maximum size within seven days, 1 uL of 10 mM GABA was added to the drop with crystals. The crystals were soaked for different time periods from 50 minutes to 2.5 hours. After soaking, crystals were transferred into a cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.
分辨率 2.20 Å R-free 0.268
7TED Human Ornithine Aminotransferase cocrystallized with its inhibitor, (S,E)-3-amino-4-(fluoromethylene)cyclopent-1-ene-1-carboxylate 提交 2022-01-04 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
链 B 36–439（404 aa）
未记录 I1T (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, OAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplied supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 was being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen
分辨率 2.63 Å R-free 0.288
7TED Human Ornithine Aminotransferase cocrystallized with its inhibitor, (S,E)-3-amino-4-(fluoromethylene)cyclopent-1-ene-1-carboxylate 提交 2022-01-04 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 36–439（404 aa）
链 I 36–439（404 aa）
未记录 I1T (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid × 1 PLP PYRIDOXAL-5'-PHOSPHATE × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, OAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplied supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 was being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen
分辨率 2.63 Å R-free 0.288
7TED Human Ornithine Aminotransferase cocrystallized with its inhibitor, (S,E)-3-amino-4-(fluoromethylene)cyclopent-1-ene-1-carboxylate 提交 2022-01-04 配体/离子不同 实验环境不同 结构质量不同 Assembly 3 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 D 36–439（404 aa）
链 E 36–439（404 aa）
未记录 I1T (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, OAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplied supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 was being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen
分辨率 2.63 Å R-free 0.288
7TED Human Ornithine Aminotransferase cocrystallized with its inhibitor, (S,E)-3-amino-4-(fluoromethylene)cyclopent-1-ene-1-carboxylate 提交 2022-01-04 配体/离子不同 实验环境不同 结构质量不同 Assembly 4 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 F 36–439（404 aa）
未记录 I1T (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, OAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplied supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 was being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen
分辨率 2.63 Å R-free 0.288
7TED Human Ornithine Aminotransferase cocrystallized with its inhibitor, (S,E)-3-amino-4-(fluoromethylene)cyclopent-1-ene-1-carboxylate 提交 2022-01-04 配体/离子不同 实验环境不同 结构质量不同 Assembly 5 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 G 36–439（404 aa）
链 H 36–439（404 aa）
未记录 I1T (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, OAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplied supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 was being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen
分辨率 2.63 Å R-free 0.288
7TEV Human Ornithine Aminotransferase cocrystallized with its inhibitor, (3S,4R)-3-amino-4-(difluoromethyl)cyclopent-1-ene-1-carboxylate 提交 2022-01-05 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 I1T (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, hOAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen.
分辨率 1.91 Å R-free 0.269
7TEV Human Ornithine Aminotransferase cocrystallized with its inhibitor, (3S,4R)-3-amino-4-(difluoromethyl)cyclopent-1-ene-1-carboxylate 提交 2022-01-05 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
链 C 36–439（404 aa）
未记录 I1T (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, hOAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen.
分辨率 1.91 Å R-free 0.269
7TFP Human Ornithine Aminotransferase cocrystallized with its inhibitor, (1S,3S)-3-amino-4-(difluoromethylene)cyclopentane-1-carboxylic acid. 提交 2022-01-06 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, hOAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen.
分辨率 2.71 Å R-free 0.268
7TFP Human Ornithine Aminotransferase cocrystallized with its inhibitor, (1S,3S)-3-amino-4-(difluoromethylene)cyclopentane-1-carboxylic acid. 提交 2022-01-06 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
链 C 36–439（404 aa）
未记录 PLP PYRIDOXAL-5'-PHOSPHATE × 2 I2V (1S,3S,4S)-3-amino-4-(fluoromethyl)cyclopentane-1-carboxylic acid × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；After purification, hOAT was buffer exchanged into the crystallization buffer (50 mM Tricine pH 7.8) supplemented with 1 mM 2-ketoglutarate. The protein was concentrated to 6.5 mg/mL. Previously reported crystallization conditions were optimized using the hanging drop vapor diffusion method by varying PEG 6000 (8-12%), NaCl (100-250 mM), and glycerol (0%-10%) with 100 mM Tricine pH 7.8 being kept constant as the buffer. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of ligand. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, and 100 mM Tricine pH 7.8. Crystals were transferred to a cryo-protectant solution (well solution supplemented with 30% glycerol) and flash-frozen in liquid nitrogen.
分辨率 2.71 Å R-free 0.268
8EZ1 Human Ornithine Aminotransferase (hOAT) co-crystallized with its inactivator 3-Amino-4-fluorocyclopentenecarboxylic Acid 提交 2022-10-30 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
链 B 36–439（404 aa）
未记录 X8B (3E,4E)-4-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-3-iminocyclopent-1-ene-1-carboxylic acid × 1 X8H (1R,3S,4Z)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The crystals with the best morphology and size grew in a final condition containing 10% PEG 6000, 100 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8.
分辨率 1.91 Å R-free 0.237
8EZ1 Human Ornithine Aminotransferase (hOAT) co-crystallized with its inactivator 3-Amino-4-fluorocyclopentenecarboxylic Acid 提交 2022-10-30 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 C 36–439（404 aa）
未记录 X8B (3E,4E)-4-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-3-iminocyclopent-1-ene-1-carboxylic acid × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；293 K；The crystals with the best morphology and size grew in a final condition containing 10% PEG 6000, 100 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8.
分辨率 1.91 Å R-free 0.237
8V9M Human Ornithine Aminotransferase cocrystallized with its inhibitor, (R)-3-amino-5,5-difluorocyclohex-1-ene-1-carboxylic acid. 提交 2023-12-08 配体/离子不同 实验环境不同 结构质量不同 Assembly 1 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 A 36–439（404 aa）
未记录 YR5 3-fluoro-5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]benzoic acid × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；10% PEG 6000, 100 mM NaCl, 20% glycerol, 100 mM tricine, pH 7.8
分辨率 1.61 Å R-free 0.193
8V9M Human Ornithine Aminotransferase cocrystallized with its inhibitor, (R)-3-amino-5,5-difluorocyclohex-1-ene-1-carboxylic acid. 提交 2023-12-08 配体/离子不同 实验环境不同 结构质量不同 Assembly 2 蛋白同源多聚体 同源多聚体；蛋白 × 2 PDB 声明：dimeric
链 B 36–439（404 aa）
链 C 36–439（404 aa）
未记录 YR5 3-fluoro-5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]benzoic acid × 2 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；10% PEG 6000, 100 mM NaCl, 20% glycerol, 100 mM tricine, pH 7.8
分辨率 1.61 Å R-free 0.193

共 26 个其他 PDB 条目、67 个 assembly。 打开独立比较页并筛选聚集状态

查看构建体与数据证据
UniProt名称 OAT_HUMAN
Isoform —
PDB实体 1
链与序列区间 作者链 A； PDB构建体 1–404； UniProt 36–439 作者链 B； PDB构建体 1–404； UniProt 36–439 作者链 C； PDB构建体 1–404； UniProt 36–439

页面优先展示蛋白身份、当前 assembly、共同组分、聚集状态和跨 PDB 结构链接。 链映射与序列区间收在“数据证据”中；数据库内部编号、导入时间和 assembly 操作表达式仅用于维护，因此不在读者页面展示。

SAXS 散射曲线 SAXS Profile

SAXS profile for 6v8d

P(r) 距离分布 P(r) Distribution

P(r) distribution for 6v8d
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2. 结构基本信息 2. Structure Basics

条目编号 entry_id6v8d
沉积日期 deposition_date2019-12-10
结构标题 titleDesign, Synthesis, and Mechanism of Fluorine-substituted Cyclohexene Analogues of GAMA-Aminobutyric Acid (GABA) as Selective Ornithine Aminotransferase Inactivators
关键词 keywordsHuman Ornithine Aminotransferase (hOAT), Mechanism Based Inactivator, PLP Hepatocellular Carcinoma (HCC), TRANSFERASE; TRANSFERASE
实验方法 methodX-RAY DIFFRACTION
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3. SAXS 参数 (CRYSOL 理论计算) 3. SAXS Parameters (CRYSOL)

回转半径 Rg (Guinier) rg_guinier34.76 Å
回转半径 Rg (电子) rg_electron34.45 Å
零角强度 I(0) i0263842000.00
分子量 molecular_weight135050.0 kDa
排除体积 excluded_volume170640 ų
包络体积 envelope_volume205230 ų
水化壳体积 shell_volume49823 ų
包络直径 envelope_diameter120.6 Å
壳层 Rg shell_rg40.80 Å
包络 Rg envelope_rg34.48 Å
形状 Rg shape_rg34.44 Å
总 Rg total_rg34.91 Å
总原子数 total_atoms9525
残基数 n_residues1206
球谐函数阶数 n_harmonics20
q 范围 q_range— – 0.5000 Å−1
数据点数 n_points101
壳层类型 shell_typedirectional
溶剂电子密度 solvent_density0.3340 e/ų
壳层衬度 contrast_shell0.0300 e/ų
CRYSOL 版本 crysol_version4.1.3
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4. P(r) 距离分布 (GNOM 反演) 4. P(r) Analysis (GNOM)

最大尺寸 Dmax dmax117.8 Å
Rg (实空间) rg_real34.85 Å
Rg 误差 (实空间) rg_real_error0.88 Å
I(0) (实空间) i0_real2.6380e+08
I(0) 误差 (实空间) i0_real_error4.1450e+06
Rg (倒空间) rg_reciprocal34.80 Å
I(0) (倒空间) i0_reciprocal263800000.0000
解质量估计 total_estimate0.8656
解质量评级 solution_quality GOOD a GOOD solution
P(r) 峰数 n_peaks1
主峰位置 r_peak_primary38.4 Å
偏度 Skewness skewness0.462
峰度 Kurtosis kurtosis-0.232
角度范围 angular_range— – 0.2300 Å−1
当前正则化参数 α current_alpha0.0001
最高正则化参数 α highest_alpha87530000.0000
实空间数据点数 n_real_points47
GNOM 版本 gnom_version4.1.3
质量判据 quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.843
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5. 晶体学与实验 5. Crystallography & Experiment

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6. 实体与聚合物信息 Entities & Polymers (4)

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7. 折叠分类 (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

结构域编号 domain_idd6v8da_
类 Class classc — Alpha and beta proteins (a/b)
折叠类型 Fold foldc.67 — PLP-dependent transferase-like
超家族 Superfamily superfamilyc.67.1 — PLP-dependent transferases
家族 Family familyc.67.1.4 — GABA-aminotransferase-like
结构域编号 domain_idd6v8db_
类 Class classc — Alpha and beta proteins (a/b)
折叠类型 Fold foldc.67 — PLP-dependent transferase-like
超家族 Superfamily superfamilyc.67.1 — PLP-dependent transferases
家族 Family familyc.67.1.4 — GABA-aminotransferase-like
结构域编号 domain_idd6v8dc_
类 Class classc — Alpha and beta proteins (a/b)
折叠类型 Fold foldc.67 — PLP-dependent transferase-like
超家族 Superfamily superfamilyc.67.1 — PLP-dependent transferases
家族 Family familyc.67.1.4 — GABA-aminotransferase-like
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8. 引用文献 (1)

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9. 文件与曲线 (10)