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4auc

Bovine chymosin in complex with Pepstatin A

Method: X-RAY DIFFRACTION Dmax: 67.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CHYMOSIN

BOS TAURUS

UniProt P00794

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 59–381 Not recorded PEPSTATIN A × 1 NA SODIUM ION × 1 CD CADMIUM ION × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.5；RESERVOIR: 75 MM BIS-TRIS PH 5.5, 0.15 M NACL, 19% (W/V) PEG3350, 7.5 MM CDCL2. SAMPLE: 7.2 MG/ML OF PROTEIN COMPLEX IN 10 MM NAH2PO4 PH 6 Resolution 1.60 Å R-free 0.197

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 4AUC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CMS THE THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT BOVINE CHYMOSIN AT 2.3 ANGSTROMS RESOLUTION Deposited 1989-10-12 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 59–381（323 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å
1CZI CHYMOSIN COMPLEX WITH THE INHIBITOR CP-113972 Deposited 1997-01-15 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 59–381（323 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 2.30 Å
3CMS ENGINEERING ENZYME SUB-SITE SPECIFICITY: PREPARATION, KINETIC CHARACTERIZATION AND X-RAY ANALYSIS AT 2.0-ANGSTROMS RESOLUTION OF VAL111PHE SITE-MUTATED CALF CHYMOSIN Deposited 1990-02-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 59–381（323 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
4AA8 Bovine chymosin at 1.8A resolution Deposited 2011-11-30 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 59–381（323 aa）
Not recorded CL CHLORIDE ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；RESERVOIR: 1.5 M NACL, 100 MM NAH2PO4, PH 5.5. SAMPLE: 30 MG/ML PROTEIN IN 50 MM NAH2PO4, PH 6.0.
Resolution 1.80 Å R-free 0.215
4CMS X-RAY ANALYSES OF ASPARTIC PROTEINASES IV. STRUCTURE AND REFINEMENT AT 2.2 ANGSTROMS RESOLUTION OF BOVINE CHYMOSIN Deposited 1991-11-01 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 59–381（323 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHYM_BOVIN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–323； UniProt 59–381

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 4auc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4auc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4auc
Deposition date deposition_date2012-05-16
Structure title titleBovine chymosin in complex with Pepstatin A
Keywords keywordsHYDROLASE-HYDROLASE INHIBITOR COMPLEX, HYDROLASE, HYDROLASE INHIBITOR, PEPTIDASE, INHIBITION; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.95 Å
Radius of gyration Rg (electron density) rg_electron19.78 Å
Forward intensity I(0) i022809800.00
Molecular weight molecular_weight36707.0 kDa
Excluded volume excluded_volume45856 ų
Envelope volume envelope_volume52390 ų
Hydration-shell volume shell_volume21963 ų
Envelope diameter envelope_diameter68.0 Å
Shell Rg shell_rg26.60 Å
Envelope Rg envelope_rg20.02 Å
Shape Rg shape_rg19.75 Å
Total Rg total_rg20.73 Å
Total atoms total_atoms2577
Residues n_residues326
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax67.0 Å
Rg (real space) rg_real20.86 Å
Rg uncertainty (real space) rg_real_error0.29 Å
I(0) (real space) i0_real2.2810e+07
I(0) uncertainty (real space) i0_real_error2.8150e+05
Rg (reciprocal space) rg_reciprocal20.88 Å
I(0) (reciprocal space) i0_reciprocal22810000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2 Å
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.365
Angular range angular_range— – 0.3800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3890000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.980
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4auca_
Class classb — All beta proteins
Fold Fold foldb.50 — Acid proteases
Superfamily Superfamily superfamilyb.50.1 — Acid proteases
Family Family familyb.50.1.2 — Pepsin-like

CATH v4.4 (2 domains)

Domain ID domain_id4aucA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily10 — Acid Proteases
Domain ID domain_id4aucA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily10 — Acid Proteases
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8. Citations (1)

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9. Files and Curves (10)