Current Protein Identity：P07824
New Search
Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1D3V CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH 2(S)-AMINO-6-BORONOHEXANOIC ACID, AN L-ARGININE ANALOG Deposited 1999-10-01 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 ABH 2(S)-AMINO-6-BORONOHEXANOIC ACID × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 8.1；pH 8.10
|
Resolution 1.70 Å R-free 0.179 |
| 1D3V CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH 2(S)-AMINO-6-BORONOHEXANOIC ACID, AN L-ARGININE ANALOG Deposited 1999-10-01 | Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain B
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 ABH 2(S)-AMINO-6-BORONOHEXANOIC ACID × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 8.1；pH 8.10
|
Resolution 1.70 Å R-free 0.179 |
| 1HQ5 CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH S-(2-BORONOETHYL)-L-CYSTEINE, AN L-ARGININE ANALOGUE Deposited 2000-12-14 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 S2C S-2-(BORONOETHYL)-L-CYSTEINE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 1500, BICINE, manganese chloride, 2-(boronoethyl)-L-cysteine, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.30 Å R-free 0.194 |
| 1HQ5 CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH S-(2-BORONOETHYL)-L-CYSTEINE, AN L-ARGININE ANALOGUE Deposited 2000-12-14 | Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain B
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 S2C S-2-(BORONOETHYL)-L-CYSTEINE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 1500, BICINE, manganese chloride, 2-(boronoethyl)-L-cysteine, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.30 Å R-free 0.194 |
| 1HQF CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH N-HYDROXY-L-ARGININE Deposited 2000-12-16 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 HAR N-OMEGA-HYDROXY-L-ARGININE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, BICINE, manganese chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.90 Å R-free 0.289 |
| 1HQG CRYSTAL STRUCTURE OF THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA Deposited 2000-12-16 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Mutation：H141C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H141C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H141C Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 6 ORN L-ornithine × 3 URE UREA × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, BICINE, manganese chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.00 Å R-free 0.232 |
| 1HQH CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH NOR-N-HYDROXY-L-ARGININE Deposited 2000-12-16 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 NNH NOR-N-OMEGA-HYDROXY-L-ARGININE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, BICINE, manganese chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.80 Å R-free 0.259 |
| 1HQX R308K ARGINASE VARIANT Deposited 2000-12-20 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Mutation：R308K Mutation：R308K Mutation：R308K | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, BICINE, manganese chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 3.00 Å R-free 0.296 |
| 1P8M Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Manganese Cluster of Arginase I. Deposited 2003-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–314（314 aa）
Fragment：Arginase I
Chain B
1–314（314 aa）
Fragment：Arginase I
Chain C
1–314（314 aa）
Fragment：Arginase I
|
Mutation：D128E Mutation：D128E Mutation：D128E | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, Bicine, Manganese Chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.84 Å R-free 0.298 |
| 1P8N Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Manganese Cluster of Arginase I. Deposited 2003-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Fragment：Arginase I
Chain B
6–319（314 aa）
Fragment：Arginase I
Chain C
6–319（314 aa）
Fragment：Arginase I
|
Mutation：D232A Mutation：D232A Mutation：D232A | MN MANGANESE (II) ION × 3 GOL GLYCEROL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, Bicine, Manganese Chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.90 Å R-free 0.305 |
| 1P8O Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Manganese Cluster of Arginase I. Deposited 2003-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Fragment：Arginase I
Chain B
6–319（314 aa）
Fragment：Arginase I
Chain C
6–319（314 aa）
Fragment：Arginase I
|
Mutation：D128N Mutation：D128N Mutation：D128N | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, Bicine, Manganese Chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.96 Å R-free 0.297 |
| 1P8P Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Manganese Cluster of Arginase I. Deposited 2003-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Fragment：Arginase I
Chain B
6–319（314 aa）
Fragment：Arginase I
Chain C
6–319（314 aa）
Fragment：Arginase I
|
Mutation：H101N Mutation：H101N Mutation：H101N | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 9；298 K；PEG 8000, Bicine, Manganese Chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.50 Å R-free 0.263 |
| 1P8Q Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Cluster of Arginase I. Deposited 2003-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Fragment：Arginase I
Chain B
6–319（314 aa）
Fragment：Arginase I
Chain C
6–319（314 aa）
Fragment：Arginase I
|
Mutation：D234E Mutation：D234E Mutation：D234E | MN MANGANESE (II) ION × 6 GOL GLYCEROL × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, Bicine, Manganese Chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.95 Å R-free 0.287 |
| 1P8R Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Manganese Cluster of Arginase I. Deposited 2003-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–313（308 aa）
Fragment：Arginase I
|
Mutation：H101E | CL CHLORIDE ION × 6 MN MANGANESE (II) ION × 6 S2C S-2-(BORONOETHYL)-L-CYSTEINE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；HEPES-NaOH, isopropanol, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.50 Å R-free 0.201 |
| 1P8R Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Manganese Cluster of Arginase I. Deposited 2003-05-07 | Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain B
6–313（308 aa）
Fragment：Arginase I
|
Mutation：H101E | CL CHLORIDE ION × 6 MN MANGANESE (II) ION × 6 S2C S-2-(BORONOETHYL)-L-CYSTEINE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；HEPES-NaOH, isopropanol, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.50 Å R-free 0.201 |
| 1P8S Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Manganese Cluster of Arginase I. Deposited 2003-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Fragment：Arginase I
Chain B
6–319（314 aa）
Fragment：Arginase I
Chain C
6–319（314 aa）
Fragment：Arginase I
|
Mutation：D232C Mutation：D232C Mutation：D232C | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, Bicine, Manganese Chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 3.20 Å R-free 0.315 |
| 1R1O Amino Acid Sulfonamides as Transition-State Analogue Inhibitors of Arginase Deposited 2003-09-24 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 SDC S-[2-(AMINOSULFONYL)ETHYL]-D-CYSTEINE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 8000, bicine, manganese chloride, SDC, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.80 Å R-free 0.290 |
| 1RLA THREE-DIMENSIONAL STRUCTURE OF RAT LIVER ARGINASE, THE BINUCLEAR MANGANESE METALLOENZYME OF THE UREA CYCLE Deposited 1996-08-15 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.10 Å R-free 0.229 |
| 1T4P Arginase-dehydro-ABH complex Deposited 2004-04-30 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 2BH [(1E,5S)-5-AMINO-5-CARBOXYPENT-1-ENYL](TRIHYDROXY)BORATE(1-) × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；278 K；bicine, PEG8000, MnCl2, dehydro-ABH, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K
|
Resolution 2.60 Å R-free 0.292 |
| 1T4R arginase-descarboxy-nor-NOHA complex Deposited 2004-04-30 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 AHI 3-{[(E)-AMINO(HYDROXYIMINO)METHYL]AMINO}PROPAN-1-AMINIUM × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；bicine, PEG8000, MnCl2, descarboxy-nor-NOHA, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.60 Å R-free 0.291 |
| 1T4S arginase-L-valine complex Deposited 2004-04-30 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 VAL VALINE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；bicine, PEG8000, L-valine, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.80 Å R-free 0.292 |
| 1T4T arginase-dinor-NOHA complex Deposited 2004-04-30 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 DIR 3-{[(E)-AMINO(HYDROXYIMINO)METHYL]AMINO}ALANINE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；bicine, PEG8000, dinor-NOHA, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.20 Å R-free 0.281 |
| 1T5F arginase I-AOH complex Deposited 2004-05-04 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Not recorded | MN MANGANESE (II) ION × 6 DHH (S)-2-AMINO-7,7-DIHYDROXYHEPTANOIC ACID × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；bicine, PEG8000, AOH, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.20 Å R-free 0.241 |
| 1T5G Arginase-F2-L-Arginine complex Deposited 2004-05-04 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Not recorded | F FLUORIDE ION × 6 MN MANGANESE (II) ION × 6 ARG ARGININE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；bicine, PEG8000, L-arginine, NaF, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.40 Å R-free 0.254 |
| 1TA1 H141C mutant of rat liver arginase I Deposited 2004-05-19 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Mutation：H141C Mutation：H141C Mutation：H141C | MN MANGANESE (II) ION × 6 GOL GLYCEROL × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；bicine, PEG8000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.50 Å R-free 0.248 |
| 1TBH H141D mutant of rat liver arginase I Deposited 2004-05-20 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Mutation：H141D Mutation：H141D Mutation：H141D | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；bicine, PEG8000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.70 Å R-free 0.296 |
| 1TBJ H141A mutant of rat liver arginase I Deposited 2004-05-20 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Mutation：H141A Mutation：H141A Mutation：H141A | MN MANGANESE (II) ION × 6 GOL GLYCEROL × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；bicine, PEG8000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.80 Å R-free 0.299 |
| 1TBL H141N mutant of rat liver arginase I Deposited 2004-05-20 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Mutation：H141N Mutation：H141N Mutation：H141N | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；bicine, PEG8000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 3.10 Å R-free 0.306 |
| 1ZPE Arginase I covalently modified with butylamine at Q19C Deposited 2005-05-16 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
6–319（314 aa）
|
Mutation：C119A, C168A, C303A, H141A, Q19(BBC) Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.4；277 K；Bicine, PEG 8000, MnCl2, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.70 Å R-free 0.233 |
| 1ZPE Arginase I covalently modified with butylamine at Q19C Deposited 2005-05-16 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain B
6–319（314 aa）
|
Mutation：C119A, C168A, C303A, H141A, Q19(BBC) Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.4；277 K；Bicine, PEG 8000, MnCl2, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.70 Å R-free 0.233 |
| 1ZPE Arginase I covalently modified with butylamine at Q19C Deposited 2005-05-16 | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain C
6–319（314 aa）
|
Mutation：C119A, C168A, C303A, H141A, Q19(BBC) Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.4；277 K；Bicine, PEG 8000, MnCl2, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.70 Å R-free 0.233 |
| 1ZPE Arginase I covalently modified with butylamine at Q19C Deposited 2005-05-16 | Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Mutation：C119A, C168A, C303A, H141A, Q19(BBC) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C119A, C168A, C303A, H141A, Q19(BBC) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C119A, C168A, C303A, H141A, Q19(BBC) Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.4；277 K；Bicine, PEG 8000, MnCl2, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.70 Å R-free 0.233 |
| 1ZPG Arginase I covalently modified with propylamine at Q19C Deposited 2005-05-16 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
6–319（314 aa）
|
Mutation：C119A, C168A, C303A, H141A, Q19C Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.4；277 K；Bicine, PEG 8000, MnCl2, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å R-free 0.220 |
| 1ZPG Arginase I covalently modified with propylamine at Q19C Deposited 2005-05-16 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain B
6–319（314 aa）
|
Mutation：C119A, C168A, C303A, H141A, Q19C Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.4；277 K；Bicine, PEG 8000, MnCl2, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å R-free 0.220 |
| 1ZPG Arginase I covalently modified with propylamine at Q19C Deposited 2005-05-16 | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain C
6–319（314 aa）
|
Mutation：C119A, C168A, C303A, H141A, Q19C Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.4；277 K；Bicine, PEG 8000, MnCl2, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å R-free 0.220 |
| 1ZPG Arginase I covalently modified with propylamine at Q19C Deposited 2005-05-16 | Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
6–319（314 aa）
Chain B
6–319（314 aa）
Chain C
6–319（314 aa）
|
Mutation：C119A, C168A, C303A, H141A, Q19C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C119A, C168A, C303A, H141A, Q19C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C119A, C168A, C303A, H141A, Q19C Non-standard monomer：Yes (specific site not provided by mmCIF) | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.4；277 K；Bicine, PEG 8000, MnCl2, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 1.90 Å R-free 0.220 |
| 2RLA ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION Deposited 1997-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Not recorded | MN MANGANESE (II) ION × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 8.5；12 - 18% PEG 8000, 50 MM BICINE PH = 8.5, 0.05% AZIDE, 1 MM MNCL2 SOAKED FOR 1 WEEK WITH 20 MM EDTA + DPA
|
Resolution 3.00 Å R-free 0.299 |
| 3E8Q X-ray structure of rat arginase I-T135A: the unliganded complex Deposited 2008-08-20 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Mutation：T135A Mutation：T135A Mutation：T135A | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；drops containing 3 microL of protein solution [5 mg/mL protein, 50 mM bicine (pH 8.5), 2 mM BEC, 2 mM MnCl2] and 3 microL of precipitant solution [0.1 M CHES (pH 9.5), 20% PEG 3350, 0.2 M NaCl] were equilibrated over a 1 mL reservoir of precipitant solution, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.90 Å R-free 0.296 |
| 3E8Z X-ray structure of rat arginase I-N130A mutant: the unliganded complex Deposited 2008-08-20 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Mutation：N130A Mutation：N130A Mutation：N130A | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；drops containing 3 microL of protein solution [5 mg/mL protein, 50 mM bicine (pH 8.5), 2 mM BEC, 2 mM MnCl2] and 3 microL of precipitant solution [0.1 M CHES (pH 9.5), 20% PEG 3350, 0.2 M NaCl] were equilibrated over a 1 mL reservoir of precipitant solution., VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.00 Å R-free 0.280 |
| 3E9B X-ray structure of rat arginase I-T135A mutant: the complex with BEC Deposited 2008-08-21 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Mutation：T135A Mutation：T135A Mutation：T135A | MN MANGANESE (II) ION × 6 S2C S-2-(BORONOETHYL)-L-CYSTEINE × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；drops containing 3 microL of protein solution [5 mg/mL protein, 50 mM bicine (pH 8.5), 2 mM BEC, 2 mM MnCl2] and 3 microL of precipitant solution [0.1 M CHES (pH 9.5), 20% PEG 8000] were equilibrated over a 1 mL reservoir of precipitant solution. , VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.15 Å R-free 0.274 |
| 3RLA ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION Deposited 1997-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Mutation：H101N Mutation：H101N Mutation：H101N | MN MANGANESE (II) ION × 6 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 8.5；12 - 18% PEG 8000, 50 MM BICINE PH = 8.5, 0.05% AZIDE, 1 MM MNCL2
|
Resolution 2.54 Å R-free 0.282 |
| 4RLA ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION Deposited 1997-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Mutation：H101N Mutation：H101N Mutation：H101N | MN MANGANESE (II) ION × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 8.5；12 - 18% PEG 8000, 50 MM BICINE PH = 8.5, 0.05% AZIDE, 1 MM MNCL2 SOAKED FOR 1 WEEK IN 15MM EDTA + DPA
|
Resolution 2.94 Å R-free 0.246 |
| 5RLA ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION Deposited 1997-05-07 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
Chain A
1–323（323 aa）
Chain B
1–323（323 aa）
Chain C
1–323（323 aa）
|
Mutation：H101N Mutation：H101N Mutation：H101N | MN MANGANESE (II) ION × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 8.5；12 - 18% PEG 8000, 50 MM BICINE PH = 8.5, 0.05% AZIDE, 1 MM MNCL2 SOAKED FOR 1 WEEK IN 15MM EDTA + DPA
|
Resolution 2.74 Å R-free 0.270 |