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- PDB-4lco: Crystal structure of NE0047 with complex with substrate ammeline -

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Basic information

Entry
Database: PDB / ID: 4lco
TitleCrystal structure of NE0047 with complex with substrate ammeline
ComponentsCytidine and deoxycytidylate deaminase zinc-binding region
KeywordsHYDROLASE / CDA fold / deaminase
Function / homology
Function and homology information


hydrolase activity / zinc ion binding
Similarity search - Function
Cytidine and deoxycytidylate deaminase zinc-binding region / Cytidine Deaminase, domain 2 / Cytidine Deaminase; domain 2 / APOBEC/CMP deaminase, zinc-binding / Cytidine and deoxycytidylate deaminases zinc-binding region signature. / Cytidine and deoxycytidylate deaminase domain / Cytidine and deoxycytidylate deaminases domain profile. / Cytidine deaminase-like / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
4,6-diamino-1,3,5-triazin-2-ol / Cytidine and deoxycytidylate deaminase zinc-binding region
Similarity search - Component
Biological speciesNitrosomonas europaea (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsBitra, A. / Biswas, A. / Anand, R.
CitationJournal: Biochemistry / Year: 2013
Title: Structural basis of the substrate specificity of cytidine deaminase superfamily Guanine deaminase
Authors: Bitra, A. / Biswas, A. / Anand, R.
History
DepositionJun 22, 2013Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jan 22, 2014Provider: repository / Type: Initial release
Revision 1.1Nov 8, 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 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _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.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.2Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytidine and deoxycytidylate deaminase zinc-binding region
B: Cytidine and deoxycytidylate deaminase zinc-binding region
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,4315
Polymers41,1732
Non-polymers2583
Water72140
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3880 Å2
ΔGint-70 kcal/mol
Surface area14640 Å2
MethodPISA
Unit cell
Length a, b, c (Å)38.030, 72.880, 109.970
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Cytidine and deoxycytidylate deaminase zinc-binding region


Mass: 20586.463 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Nitrosomonas europaea (bacteria) / Strain: ATCC 19718 / NBRC 14298 / Gene: NE0047 / Production host: Escherichia coli (E. coli)
References: UniProt: Q82Y41, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-6AM / 4,6-diamino-1,3,5-triazin-2-ol / Ammeline


Mass: 127.105 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N5O
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 40 / 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: 1.85 Å3/Da / Density % sol: 33.54 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.225M MgCl2, 25% PEG 3350, 0.1M Bis-Tris (pH 5.5), pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 14, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 2.7→43.89 Å / Num. all: 8919 / Num. obs: 8919 / % possible obs: 100 % / Redundancy: 8.7 % / Rmerge(I) obs: 0.149 / Net I/σ(I): 11.7
Reflection shellResolution: 2.7→2.85 Å / Redundancy: 8.6 % / Rmerge(I) obs: 0.423 / Mean I/σ(I) obs: 4.8 / % possible all: 100

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Processing

Software
NameVersionClassificationNB
REFMAC5.6.0117refinement
PDB_EXTRACT3.11data extraction
iMOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2G84

2g84


Resolution: 2.7→43.89 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.892 / Occupancy max: 1 / Occupancy min: 0.3 / SU B: 13.157 / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.405 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES: REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2399 1123 12.6 %RANDOM
Rwork0.1704 ---
obs0.1795 8880 99.94 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 94.87 Å2 / Biso mean: 24.9242 Å2 / Biso min: 6.48 Å2
Baniso -1Baniso -2Baniso -3
1--1.57 Å20 Å20 Å2
2--4.19 Å20 Å2
3----2.62 Å2
Refinement stepCycle: LAST / Resolution: 2.7→43.89 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2713 0 11 40 2764
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0192773
X-RAY DIFFRACTIONr_angle_refined_deg1.5131.9743779
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.6435369
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.49323.391115
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.2815411
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.4751525
X-RAY DIFFRACTIONr_chiral_restr0.0930.2435
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0212146
LS refinement shellResolution: 2.7→2.77 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.291 86 -
Rwork0.221 465 -
all-551 -
obs--99.82 %

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