PROTEIN (METHIONINE AMINOPEPTIDASE)
Escherichia coli
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 1–264 | Mutation：R175Q | CO COBALT (II) ION × 3 NA SODIUM ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.1；CRYSTALS OF THE CO(II)-SUBSTITUTED ENZYME WERE GROWN AT ROOM TEMPERATURE BY VAPOR DIFFUSION IN 20-30 UL SITTING DROPS AFTER MIXING THE PROTEIN, 12 MG/ML SOLUTION IN STORAGE BUFFER(25 MM HEPES PH 6.8, 25 MM K2SO4, 100 MM NACL, 1 MM COCL2, 15 MM METHIONINE),CONTAINING 48.8 MM N-OCTANOYL SUCROSE, 1:1 WITH WELL SOLUTIONS (24-26% PEG4000, 0.1M HEPES PH7.0-7.2,FRESH 2 MM COCL2)., pH 7.1, VAPOR DIFFUSION, HANGING DROP | Resolution 1.90 Å |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
| Other PDB | Difference from Current Entry 2MAT | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1C21 E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE COMPLEX Deposited 1999-07-22 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–264（263 aa）
Fragment：METHIONINE
|
Mutation：R175Q | CO COBALT (II) ION × 2 NA SODIUM ION × 1 MET METHIONINE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；K2SO4, NaCl, methionine, N-octanoyl sucrose, PEG 4000, HEPES, CoCl2, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.80 Å |
| 1C22 E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX Deposited 1999-07-22 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–264（263 aa）
|
Mutation：R175Q | CO COBALT (II) ION × 2 NA SODIUM ION × 1 MF3 2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；HEPES, CoCl2, K2SO4, Methionine, PEG4000, NaCl, N-octanoyl sucrose, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.75 Å |
| 1C23 E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE PHOSPHONATE COMPLEX Deposited 1999-07-22 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–264（263 aa）
|
Mutation：R175Q | CO COBALT (II) ION × 2 NA SODIUM ION × 1 MPH (1-AMINO-3-METHYLSULFANYL-PROPYL)-PHOSPHONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；Hepes, NaCl, K2SO4, CoCl2, PEG 4000, methionine, N-octanoyl sucrose, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 2.00 Å |
| 1C24 E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE PHOSPHINATE COMPLEX Deposited 1999-07-22 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–264（263 aa）
Fragment：METHIONINE PHOSPHINATE
|
Mutation：R175Q | CO COBALT (II) ION × 2 NA SODIUM ION × 1 MPJ (1-AMINO-3-METHYLSULFANYL-PROPYL)-PHOSPHINIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；Hepes, NaCl, CoCl2, K2SO4, PEG 4000, N-octanoyl sucrose, methionine, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.70 Å |
| 1C27 E. COLI METHIONINE AMINOPEPTIDASE:NORLEUCINE PHOSPHONATE COMPLEX Deposited 1999-07-22 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–264（263 aa）
Fragment：NORLEUCINE PHOSPHONATE
|
Mutation：R175Q | CO COBALT (II) ION × 2 NA SODIUM ION × 1 NLP (1-AMINO-PENTYL)-PHOSPHONIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；Hepes, NaCl, CoCl2, K2SO4, methionine, N-octanoyl sucrose, PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 298K
|
Resolution 1.95 Å |
| 1MAT STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME Deposited 1992-12-02 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–264（264 aa）
|
Not recorded | CO COBALT (II) ION × 2 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.40 Å |
| 1XNZ Crystal Structure of Mn(II) form of E. coli. Methionine Aminopeptidase in complex with 5-(2-chlorophenyl)furan-2-carboxylic acid Deposited 2004-10-05 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–264（264 aa）
|
Not recorded | MN MANGANESE (II) ION × 2 NA SODIUM ION × 1 FCD 5-(2-CHLOROPHENYL)FURAN-2-CARBOXYLIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 7.5；292 K；15% PEG 8000, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, temperature 292K
|
Resolution 1.52 Å R-free 0.250 |
| 1YVM E. coli Methionine Aminopeptidase in complex with thiabendazole Deposited 2005-02-16 | Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–264（264 aa）
|
Mutation：R175Q | CO COBALT (II) ION × 4 NA SODIUM ION × 1 TMG 2-(1,3-THIAZOL-4-YL)-1H-BENZIMIDAZOLE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.1；293 K；PEG 4000, cobalt chloride, hepes, methionine, sodium chloride, potassium chloride, pH 7.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 1.60 Å R-free 0.233 |
| 2BB7 Mn Form Of E. coli Methionine Aminopeptidase In Complex With a quinolinyl sulfonamide inhibitor Deposited 2005-10-17 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–264（264 aa）
|
Not recorded | MN MANGANESE (II) ION × 3 NA SODIUM ION × 1 QMS N-(QUINOLIN-8-YL)METHANESULFONAMIDE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；PEG 20000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 1.70 Å R-free 0.233 |
| 3MAT E.COLI METHIONINE AMINOPEPTIDASE TRANSITION-STATE INHIBITOR COMPLEX Deposited 1999-03-29 | Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
1–264（264 aa）
|
Mutation：R175Q | CO COBALT (II) ION × 2 NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.1；CRYSTALS OF THE CO(II)-SUBSTITUTED ENZYME
WERE GROWN AT ROOM TEMPERATURE BY VAPOR
DIFFUSION IN 20-30 UL SITTING DROPS AFTER
MIXING THE PROTEIN, 12 MG/ML SOLUTION IN
STORAGE BUFFER(25 MM HEPES PH 6.8, 25 MM
K2SO4, 100 MM NACL, 1 MM COCL2, 15 MM
METHIONINE),CONTAINING 48.8 MM N-OCTANOYL
SUCROSE, 1:1 WITH WELL SOLUTIONS (24-26%
PEG4000, 0.1M HEPES PH7.0-7.2,FRESH
2 MM COCL2). CRYSTALS WERE OBTAINED OF THE
INHIBITOR COMPLEX BY INCUBATING THE PROTEIN
AS ABOVE AT ROOM TEMPERATURE FOR 5 MIN WITH
A 20-FOLD MOLAR EXCESS OF THE INHIBITOR DISSOLVED
IN DMSO. THE FINAL INHIBITOR:ENZYME RATIO
WAS 10:1 (1% DMSO) AFTER MIXING THE PREFORMED
COMPLEX WITH WELL SOLUTION (0.1M MES PH 6.1,
|
Resolution 2.00 Å |
| 4MAT E.COLI METHIONINE AMINOPEPTIDASE HIS79ALA MUTANT Deposited 1999-03-29 | Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–264（264 aa）
|
Mutation：R175Q, H79A | NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；Crystals of the HIS79ALA mutant were obtained by mixing the apoenzyme
retaining the C-terminal HISs-tag (6.7 mg/ml, 20 mM DTT, 25 mM HEPES
pH 6.8, 25 mM K2SO4, 100 mM NaCl) with an equal volume of well solution
(22-27 % PEG 3400, 0.1 M HEPES pH 7.0, 200 mM NaCl). Diffraction quality
crystals were obtained after macroseeding into 20 uL hanging drops.
|
Resolution 2.00 Å |
11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | AMPM_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–264； UniProt 1–264 |
