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- PDB-3huv: Carboxypeptidase A liganded to an organic small-molecule: conform... -

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Basic information

Entry
Database: PDB / ID: 3huv
TitleCarboxypeptidase A liganded to an organic small-molecule: conformational changes
ComponentsCarboxypeptidase A1 (Pancreatic)
KeywordsHYDROLASE / CPA / M14 protease / metallocarboxypeptidase / Carboxypeptidase
Function / homology
Function and homology information


carboxypeptidase A / metallocarboxypeptidase activity / proteolysis / extracellular space / zinc ion binding
Similarity search - Function
Carboxypeptidase A, carboxypeptidase domain / Carboxypeptidase, activation peptide / Metallocarboxypeptidase-like, propeptide / Carboxypeptidase activation peptide / Zinc carboxypeptidases, zinc-binding region 2 signature. / Zinc carboxypeptidases, zinc-binding region 1 signature. / Zn_pept / Peptidase M14, carboxypeptidase A / Zinc carboxypeptidase / Zn peptidases ...Carboxypeptidase A, carboxypeptidase domain / Carboxypeptidase, activation peptide / Metallocarboxypeptidase-like, propeptide / Carboxypeptidase activation peptide / Zinc carboxypeptidases, zinc-binding region 2 signature. / Zinc carboxypeptidases, zinc-binding region 1 signature. / Zn_pept / Peptidase M14, carboxypeptidase A / Zinc carboxypeptidase / Zn peptidases / Aminopeptidase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesBos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsFernandez, D. / Boix, E. / Aviles, F.X. / Vendrell, J.
CitationJournal: To be Published
Title: Carboxypeptidase A liganded to an organic small-molecule: conformational changes
Authors: Fernandez, D.
History
DepositionJun 15, 2009Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jun 2, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_source / pdbx_initial_refinement_model / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Carboxypeptidase A1 (Pancreatic)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,7872
Polymers34,7221
Non-polymers651
Water3,999222
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)42.830, 56.980, 56.690
Angle α, β, γ (deg.)90.00, 100.25, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Carboxypeptidase A1 (Pancreatic)


Mass: 34721.750 Da / Num. of mol.: 1 / Fragment: UNP residues 111-419
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Gene: CPA1 / Plasmid: pPIC9 / Production host: Pichia pastoris (fungus) / Strain (production host): KM71 / References: UniProt: A6H6Y4
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 222 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 1.96 Å3/Da / Density % sol: 37.26 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 10% PEG8000, 0.02M tris, pH7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.8148 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Jun 29, 2007
RadiationMonochromator: Si (111), horizontally focussing / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8148 Å / Relative weight: 1
ReflectionResolution: 1.9→55.815 Å / Num. all: 21281 / Num. obs: 21263 / % possible obs: 99.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.3 % / Biso Wilson estimate: 16.03 Å2 / Rmerge(I) obs: 0.164 / Rsym value: 0.136 / Net I/σ(I): 9.6
Reflection shellResolution: 1.9→2 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 2.4 / Num. unique all: 3091 / Rsym value: 0.49 / % possible all: 100

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
PHASERphasing
REFMAC5.5.0066refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2CTB

2ctb


Resolution: 1.9→21 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.925 / SU B: 3.731 / SU ML: 0.106 / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / ESU R: 0.175 / ESU R Free: 0.154 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS; TYR248 RESIDUE IS RELATED TO CPA CATALYTIC MECHANISM. VERY WEAK ELECTRON DENSITY FOR TYR248 SIDE CHAIN WAS FOUND. SIDE CHAIN ATOMS WERE ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS; TYR248 RESIDUE IS RELATED TO CPA CATALYTIC MECHANISM. VERY WEAK ELECTRON DENSITY FOR TYR248 SIDE CHAIN WAS FOUND. SIDE CHAIN ATOMS WERE MODELLED FROM THE SECOND MOST POPULATED ROTAMER FROM THE REFINEMENT PROGRAM WITH THE PHENOLIC HYDROXYL GROUP POINTING TOWARDS THE SOLVENT.
RfactorNum. reflection% reflectionSelection details
Rfree0.22703 450 2.1 %RANDOM
Rwork0.18169 ---
obs0.18265 20797 99.78 %-
all-21312 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 18.045 Å2
Baniso -1Baniso -2Baniso -3
1--0.34 Å20 Å2-2.16 Å2
2---1.16 Å20 Å2
3---0.73 Å2
Refinement stepCycle: LAST / Resolution: 1.9→21 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2404 0 1 222 2627
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0222463
X-RAY DIFFRACTIONr_angle_refined_deg1.1821.9283354
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.5215304
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.13723.784111
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.7715385
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.751510
X-RAY DIFFRACTIONr_chiral_restr0.0780.2368
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0211884
X-RAY DIFFRACTIONr_mcbond_it0.5141.51505
X-RAY DIFFRACTIONr_mcangle_it0.93122434
X-RAY DIFFRACTIONr_scbond_it1.4243958
X-RAY DIFFRACTIONr_scangle_it2.2424.5919
LS refinement shellResolution: 1.9→1.949 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.297 38 -
Rwork0.262 1531 -
obs--99.94 %

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