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Yorodumi- PDB-1acb: CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1acb | ||||||
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Title | CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION | ||||||
Components |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEASE / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information chymotrypsin / serpin family protein binding / digestion / serine protease inhibitor complex / response to wounding / serine-type endopeptidase inhibitor activity / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) Hirudo medicinalis (medicinal leech) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Bolognesi, M. / Frigerio, F. / Coda, A. / Pugliese, L. / Lionetti, C. / Menegatti, E. / Amiconi, G. / Schnebli, H.P. / Ascenzi, P. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992 Title: Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution. Authors: Frigerio, F. / Coda, A. / Pugliese, L. / Lionetti, C. / Menegatti, E. / Amiconi, G. / Schnebli, H.P. / Ascenzi, P. / Bolognesi, M. #1: Journal: J.Mol.Recog. / Year: 1990 Title: X-Ray Crystal Structure of the Bovine Alpha-Chymotrypsin(Slash)Eglin C Complex at 2.6 Angstroms Resolution Authors: Bolognesi, M. / Pugliese, L. / Gatti, G. / Frigerio, F. / Coda, A. / Antolini, L. / Schnebli, H.P. / Menegatti, E. / Amiconi, G. / Ascenzi, P. #2: Journal: J.Mol.Biol. / Year: 1989 Title: Preliminary Crystallographic Data on the Complex of Bovine Alpha-Chymotrypsin with the Recombinant Proteinase Inhibitor Eglin C from Hirudo Medicinalis Authors: Pugliese, L. / Gatti, G. / Bolognesi, M. / Coda, A. / Menegatti, E. / Schnebli, H.P. / Ascenzi, P. / Amiconi, G. | ||||||
History |
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Remark 700 | SHEET THE SHEETS PRESENTED AS *CH1* AND *CH2* ON SHEET RECORDS BELOW ARE ACTUALLY SIX-STRANDED BETA- ...SHEET THE SHEETS PRESENTED AS *CH1* AND *CH2* ON SHEET RECORDS BELOW ARE ACTUALLY SIX-STRANDED BETA-BARRELS. THIS IS REPRESENTED BY SEVEN-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1acb.cif.gz | 69.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1acb.ent.gz | 55 KB | Display | PDB format |
PDBx/mmJSON format | 1acb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1acb_validation.pdf.gz | 432 KB | Display | wwPDB validaton report |
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Full document | 1acb_full_validation.pdf.gz | 442.5 KB | Display | |
Data in XML | 1acb_validation.xml.gz | 16.1 KB | Display | |
Data in CIF | 1acb_validation.cif.gz | 22.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ac/1acb ftp://data.pdbj.org/pub/pdb/validation_reports/ac/1acb | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES WITH POOR ELECTRON DENSITY: SER E 77, GLU E 78, ARG E 145, ALA E 149, ASN E 150, ARG E 154, GLN E 239, LYS I 8, HIS I 28, TYR I 49, ASN I 50. |
-Components
#1: Protein | Mass: 25686.037 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin | ||
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#2: Protein | Mass: 8100.011 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hirudo medicinalis (medicinal leech) / References: UniProt: P01051 | ||
#3: Water | ChemComp-HOH / | ||
Compound details | EGLIN C IS BOUND NON-COVALENTLYSequence details | RESIDUES THR I 1, GLU I 2, PHE I 3, GLY I 4, SER I 5, GLU I 6, AND LEU I 7 OF EGLIN C HAVE BEEN ...RESIDUES THR I 1, GLU I 2, PHE I 3, GLY I 4, SER I 5, GLU I 6, AND LEU I 7 OF EGLIN C HAVE BEEN PROTEOLYTI | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.68 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion, sitting drop / Details: referred to J.Mol.Biol. 208.511-513 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 11 Å / Num. obs: 16841 / Observed criterion σ(I): 5 / Num. measured all: 31318 / Rmerge(I) obs: 0.04 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→11 Å / Rfactor obs: 0.167 / σ(F): 0 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→11 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 11 Å / Num. reflection all: 16833 / σ(F): 0 / Rfactor all: 0.167 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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